| General information | | DisProt: | DP00738 | | Name: | Pectate lyase | | Synonym(s): | Q9RHW0_BACSP
Pel-15
| | First appeared in release: | Release 6.01 (10/15/2012) | | UniProt: | Q9RHW0 | | UniGene: | | | SwissProt: | Q9RHW0_BACSP | | TrEMBL: | | | NCBI (GI): | | | Source organism: | Bacillus sp. strain KSM-P15 | | Sequence length: | 224 | | Percent disordered: | 8% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MKKLLGLILS AALTLSLYGL EPQVAEAAPT VVHETIRVPA GQTFDGKGQT YVANPNTLGD - 60
GSQAENQKPI FRLEAGASLK NVVIGAPAAD GVHCYGDCTI TNVIWEDVGE DALTLKSSGT - 120
VNISGGAAYK AYDKVFQINA AGTINIRNFR ADDIGKLVRQ NGGTTYKVVM NVENCNISRV - 180
KDAILRTDSS TSTGRIVNTR YSNVPTLFKG FKSGNTTASG NTQY
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| Functional narrative |
"Pectate lyases (Pel; E.C. 4.2.2.2) catalyze the degradation of
the pectate component of the middle lamellae and cell walls of
higher plants. The enzymes are secreted by bacteria and fungal
pathogens and cause soft-rot diseases in higher plant cells.
Generally, Pels degrade polygalacturonic acid (PGA) through
a -elimination mechanism with the assistance of Ca2+ ions at
pHs between 8 and 10." (Akita et al, 2001 Acta Cryst. D57, pp.1786)
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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: | Disordered | | Name: | disordered loop | | Location: | 53 - 70 | | Length: | 18 | | Region sequence: |
ANPNTLGDGSQAENQKPI | | Modification type: | Native
| | PDB: | 1EE6:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Substrate/ligand binding
| Detection methods:
- X-ray crystallography (277 K; pH: 6.7; PEG 8000; Pel-15)
| References:
- Akita M, Suzuki A, Kobayashi T, Ito S, Yamane T. "The first structure of pectate lyase belonging to polysaccharide lyase family 3." Acta Crystallogr. D Biol. Crystallogr.. 2001; 57(Pt 12): 1786-92. PubMed: 11717490
| Comments:Akita et al (2001) describe the structure of Pel-15 as "a simple
eight-turn parallel beta-helix with no alpha-helix."
Region 1 represents the longest loop of Turn 3 (T3) of Pel-15 structure. According to Akita et al (2001), this loop is stabilized indirectly by a calcium ion not present in other know pectate lyase structures; this calcium ion is "structurally essential for Pel-15, which is a unique feature of Pel-15."
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| Comments |
AV sent 10/3/2012 (PMID 11717490)
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