| General information | | DisProt: | DP00416 | | Name: | Acyl carrier protein | | Synonym(s): | ACP_ECOLI
ACP
Cytosolic-activating factor
CAF
Fatty acid synthase acyl carrier protein
| | First appeared in release: | Release 5.5 (11/17/2010) | | UniProt: | P0A6A8 | | UniGene: | | | SwissProt: | ACP_ECOLI | | TrEMBL: | | | NCBI (GI): | 67462084 | | Source organism: | Escherichia coli | | Sequence length: | 78 | | Percent disordered: | 44% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MSTIEERVKK IIGEQLGVKQ EEVTNNASFV EDLGADSLDT VELVMALEEE FDTEIPDEEA - 60
EKITTVQAAI DYINGHQA
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| Functional narrative |
Acyl carrier protein is the carrier of the growing fatty acid chain in fatty acid biosynthesis, and an important cofactor in numerous reactions requiring acyl transfer. The intermediates of fatty acid biosynthesis are bound to this heat-stable protein cofactor.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Ordered | | Name: | Helix alpha-1 | | Location: | 4 - 16 | | Length: | 13 | | Region sequence: |
IEERVKKIIGEQL | | Modification type: | Engineered
| | PDB: | 1L0H:A, 1L0I:A | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (290 K; pH: 6; PEG 2000; sodium cacodylate; zinc chloride)
| References:
- Roujeinikova A, Baldock C, Simon WJ, Gilroy J, Baker PJ, Stuitje AR, Rice DW, Slabas AR, Rafferty JB. "X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site." Structure. 2002; 10(6): 825-35. PubMed: 12057197
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | loop alpha-1,alpha-2 | | Location: | 17 - 36 | | Length: | 20 | | Region sequence: |
GVKQEEVTNNASFVEDLGAD | | Modification type: | Engineered
| | PDB: | 1L0H:A, 1L0I:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Fatty acylation (myristolation and palmitoylation)
Protein-lipid interaction
| Detection methods:
- X-ray crystallography (290 K; pH: 6; PEG 2000; sodium cacodylate; zinc chloride)
| References:
- Roujeinikova A, Baldock C, Simon WJ, Gilroy J, Baker PJ, Stuitje AR, Rice DW, Slabas AR, Rafferty JB. "X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site." Structure. 2002; 10(6): 825-35. PubMed: 12057197
| Comments:Roujeinikova et al (2002) suggest that this flexible loop region aids ACP in handling long fatty acyl chains.
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| Region 3 | | Type: | Ordered | | Name: | Helix alpha-2 | | Location: | 37 - 51 | | Length: | 15 | | Region sequence: |
SLDTVELVMALEEEF | | Modification type: | Engineered
| | PDB: | 1L0H:A, 1L0I:A | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Fatty acylation (myristolation and palmitoylation)
Protein-lipid interaction
| Detection methods:
- X-ray crystallography (290 K; pH: 6; PEG 2000; sodium cacodylate; zinc chloride)
| References:
- Roujeinikova A, Baldock C, Simon WJ, Gilroy J, Baker PJ, Stuitje AR, Rice DW, Slabas AR, Rafferty JB. "X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site." Structure. 2002; 10(6): 825-35. PubMed: 12057197
| Comments:Roujeinikova et al (2002), describe a hydrophobic pocket formed by the Region 3 Helix alpha-2 and Region 4 Helix alpha-3. During biosynthesis, the growing fatty acyl chain embeds in the pocket, likely for protection from unintended interactions.
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| Region 4 | | Type: | Disordered w/ Residual Structure | | Name: | flexible segment & H alpha-3 | | Location: | 52 - 65 | | Length: | 14 | | Region sequence: |
DTEIPDEEAEKITT | | Modification type: | Engineered
| | PDB: | 1L0H:A, 1L0I:A | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Fatty acylation (myristolation and palmitoylation)
Protein-lipid interaction
| Detection methods:
- X-ray crystallography (290 K; pH: 6; PEG 2000; sodium cacodylate; zinc chloride)
| References:
- Roujeinikova A, Baldock C, Simon WJ, Gilroy J, Baker PJ, Stuitje AR, Rice DW, Slabas AR, Rafferty JB. "X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site." Structure. 2002; 10(6): 825-35. PubMed: 12057197
| Comments:According to Roujeinikova et al (2002), Region 3 is a highly flexible segment that contains a small helix at aa 57-62, which the authors call Helix alpha-3. This region forms a "lid" over one wall of the hydrophobic pocket, and could be important to ACP's ability to handle varying lengths of fatty acyl chains.
Roujeinikova et al (2002), describe a hydrophobic pocket formed by the Region 3 Helix alpha-2 and Region 4 Helix alpha-3. During biosynthesis, the growing fatty acyl chain embeds in the pocket, likely for protection from unintended interactions.
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| Region 5 | | Type: | Ordered | | Name: | helix alpha-4 | | Location: | 66 - 76 | | Length: | 11 | | Region sequence: |
VQAAIDYINGH | | Modification type: | Engineered
| | PDB: | 1L0H:A, 1L0I:A | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (290 K; pH: 6; PEG 2000; sodium cacodylate; zinc chloride)
| References:
- Roujeinikova A, Baldock C, Simon WJ, Gilroy J, Baker PJ, Stuitje AR, Rice DW, Slabas AR, Rafferty JB. "X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site." Structure. 2002; 10(6): 825-35. PubMed: 12057197
| Comments:
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| References |
- Kim Y, Prestegard JH. "Refinement of the NMR structures for acyl carrier protein with scalar coupling data." Proteins. 1990; 8(4): 377-85. PubMed: 2091027
- Roujeinikova A, Baldock C, Simon WJ, Gilroy J, Baker PJ, Stuitje AR, Rice DW, Slabas AR, Rafferty JB. "X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site." Structure. 2002; 10(6): 825-35. PubMed: 12057197
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| Comments |
Proteins used by Roujeinikova et al (2002) were butyryl-ACP, SeMet butyryl-ACP and an engineered mutant SeMet butyryl-ACP I62M (I63M in UniProt aa numbering). NOTE on AA POSITIONS: The UniProt sequence includes a methionine at aa position 1, which the authors do not include in their aa numbering; the DisProt record is 'translated' to UniProt numbering.
The two PDB structures characterized by Roujeinikova et al (2002) represent a fatty acyl chain resident in the hydrophobic pocket of ACP (PDB 1L0H) and ACP with a condensed hydrophobic pocket, presumably empty after delivery of the fatty acyl chain to its partner enzyme (PDB 1L0I).
For solution NMR of ACP, see PDB entry 1ACP, the primary citation of which is Kim and Prestegard (1990), PubMed 2091027.
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