DP00618: Alpha-1,2-mannosyltransferase ALG11FASTA viewXML view

General information
DisProt:DP00618
Name:Alpha-1,2-mannosyltransferase ALG11
Synonym(s):ALG11_YEAST
Asparagine-linked glycosylation protein 11
Alg11
First appeared in release:Release 5.2 (08/07/2010)
UniProt:P53954
UniGene: 
SwissProt: ALG11_YEAST
TrEMBL:  
NCBI (GI): 1730730
Source organism:Saccharomyces cerevisiae (Baker's yeast)
Sequence length:548
Percent disordered:3%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MGSAWTNYNF EEVKSHFGFK KYVVSSLVLV YGLIKVLTWI FRQWVYSSLN PFSKKSSLLN - 60
RAVASCGEKN VKVFGFFHPY CNAGGGGEKV LWKAVDITLR KDAKNVIVIY SGDFVNGENV - 120
TPENILNNVK AKFDYDLDSD RIFFISLKLR YLVDSSTWKH FTLIGQAIGS MILAFESIIQ - 180
CPPDIWIDTM GYPFSYPIIA RFLRRIPIVT YTHYPIMSKD MLNKLFKMPK KGIKVYGKIL - 240
YWKVFMLIYQ SIGSKIDIVI TNSTWTNNHI KQIWQSNTCK IIYPPCSTEK LVDWKQKFGT - 300
AKGERLNQAI VLAQFRPEKR HKLIIESFAT FLKNLPDSVS PIKLIMAGST RSKQDENYVK - 360
SLQDWSENVL KIPKHLISFE KNLPFDKIEI LLNKSTFGVN AMWNEHFGIA VVEYMASGLI - 420
PIVHASAGPL LDIVTPWDAN GNIGKAPPQW ELQKKYFAKL EDDGETTGFF FKEPSDPDYN - 480
TTKDPLRYPN LSDLFLQITK LDYDCLRVMG ARNQQYSLYK FSDLKFDKDW ENFVLNPICK - 540
LLEEEERG



Functional narrative    

Required for N-linked oligosaccharide assembly. Has a role in the last step of the synthesis of the Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum.

Region 1: 79-92

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.


Region 1
Type:Disordered
Name:G-loop
Location:79 - 92
Length:14
Region sequence:

PYCNAGGGGEKVLW

Modification type: Native
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Substrate/ligand binding
Detection methods:
  1. Immunochemistry (298 K; KCl (buffer) 0.5 M)

References:
  1. Absmanner B, Schmeiser V, Kampf M, Lehle L. "Biochemical characterization, membrane association and identification of amino acids essential for function of Alg11 from Saccharomyces cerevisiae, an alpha1,2-mannosyltransferase, catalyzing two sequential glycosylation steps in the formation of the lipid-linked core oligosaccharide." Biochem J. 2010; 426(2): 205-17. PubMed: 19929855

  2. Breton C, Snajdrov√° L, Jeanneau C, Koca J, Imberty A. "Structures and mechanisms of glycosyltransferases." Glycobiology. 2005; 16(2): 29R-37R. PubMed: 16037492

  3. Hu Y, Chen L, Ha S, Gross B, Falcone B, Walker D, Mokhtarzadeh M, Walker S. "Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases." Proc. Natl. Acad. Sci. U.S.A.. 2003; 100(3): 845-9. PubMed: 12538870

  4. Qasba PK, Ramakrishnan B, Boeggeman E. "Substrate-induced conformational changes in glycosyltransferases." Trends Biochem. Sci.. 2005; 30(1): 53-62. PubMed: 15653326

  5. Wrabl JO, Grishin NV. "Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily." J. Mol. Biol.. 2001; 314(3): 365-74. PubMed: 11846551

Comments:
Absmanner, et al. (2010), found that replacement of glycine residues G84, G85 and G87 with alanine, there was no loss of function. When these residues were replaced with proline, G85 and G87 were found to be critical to function, but G84 was not.




References

  1. Absmanner B, Schmeiser V, Kampf M, Lehle L. "Biochemical characterization, membrane association and identification of amino acids essential for function of Alg11 from Saccharomyces cerevisiae, an alpha1,2-mannosyltransferase, catalyzing two sequential glycosylation steps in the formation of the lipid-linked core oligosaccharide." Biochem J. 2010; 426(2): 205-17. PubMed: 19929855



Comments


AV (7-7-2010) PubMed: 15653326



[ PMID 19929855]


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