PDBsum entry 2vsn

Transferase

PDB id

2vsn

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Contents

			Protein chains

					534 a.a. *

			Ligands

					UDP ×2

			Waters ×71

* Residue conservation analysis

PDB id:

2vsn

Links

Name:

Transferase

Title:

Structure and topological arrangement of an o-glcnac transferase homolog: insight into molecular control of intracellular glycosylation

Structure:

Xcogt. Chain: a, b. Engineered: yes. Mutation: yes

Source:

Xanthomonas campestris pv. Campestris. Organism_taxid: 314565. Strain: 8004. Atcc: 33913. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.75Å

R-factor:

0.241

R-free:

0.265

Authors:

C.Martinez-Fleites,M.S.Macauley,Y.He,D.Shen,D.Vocadlo,G.J.Davies

Key ref:

C.Martinez-Fleites et al. (2008). Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation. Nat Struct Biol, 15, 764-765. PubMed id: 18536723 DOI: 10.1038/nsmb.1443

Date:

28-Apr-08

Release date:

10-Jun-08

PROCHECK

	Headers

	References

Protein chains

A0A0H2XAK3 (A0A0H2XAK3_XANC8) - protein O-GlcNAc transferase from Xanthomonas campestris pv. campestris (strain 8004)

Seq: Struc:

Seq: Struc:					568 a.a. 534 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)



		Enzyme reactions

Enzyme class:

E.C.2.4.1.255 - protein O-GlcNAc transferase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

1.	L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl- beta-D-glucosaminyl)-L-seryl-[protein] + UDP + H⁺
2.	L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O- (N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + UDP + H⁺

L-seryl-[protein]	+	UDP-N-acetyl-alpha-D-glucosamine	=	3-O-(N-acetyl- beta-D-glucosaminyl)-L-seryl-[protein]	+	UDP	+	H(+)

L-threonyl-[protein]	+	UDP-N-acetyl-alpha-D-glucosamine	=	3-O- (N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein]	+	UDP	+	H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1038/nsmb.1443	Nat Struct Biol 15:764-765 (2008)
PubMed id: 18536723

Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation.
C.Martinez-Fleites, M.S.Macauley, Y.He, D.L.Shen, D.J.Vocadlo, G.J.Davies.

ABSTRACT

N-Acetylglucosamine (O-GlcNAc) modification of proteins provides a mechanism for the control of diverse cellular processes through a dynamic interplay with phosphorylation. UDP-GlcNAc:polypeptidyl transferase (OGT) catalyzes O-GlcNAc addition. The structure of an intact OGT homolog and kinetic analysis of human OGT variants reveal a contiguous superhelical groove that directs substrates to the active site.

Selected figure(s)



	Figure 1. (a) Schematic cartoon of XcOGT. UDP is shown in ball-and-stick representation with 2F[o] – F[c] electron density at 1 . The catalytic base, His218 (HsOGT His558) is shown, along with the predicted location of the putative HsOGT phosphatidylinositol 3,4,5-trisphosphate (PIP) interaction site and the interdomain insertion. (b) The XcOGT active center and interactions of UDP.		Figure 2. (a) Western blot showing expression levels of OGT variants compared to wild type (WT). (b) Michaelis-Menten kinetics (s.d. shown) for WT and selected mutant OGTs (Supplementary Table 2 and Supplementary Methods online).

Literature references that cite this PDB file's key reference

PubMed id

Reference

21327254

C.Smet-Nocca, M.Broncel, J.M.Wieruszeski, C.Tokarski, X.Hanoulle, A.Leroy, I.Landrieu, C.Rolando, G.Lippens, and C.P.Hackenberger (2011).
Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.

Mol Biosyst, 7, 1420-1429.

21295698

F.Capotosti, S.Guernier, F.Lammers, P.Waridel, Y.Cai, J.Jin, J.W.Conaway, R.C.Conaway, and W.Herr (2011).
O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1.

Cell, 144, 376-388.

20640461

H.C.Dorfmueller, V.S.Borodkin, D.E.Blair, S.Pathak, I.Navratilova, and D.M.van Aalten (2011).
Substrate and product analogues as human O-GlcNAc transferase inhibitors.

Amino Acids, 40, 781-792.

PDB codes:

2xgm 2xgo 2xgs

21321551

L.M.Gay, X.Zheng, and D.M.van Aalten (2011).
Molecular recognition: O-GlcNAc transfer: size matters.

Nat Chem Biol, 7, 134-135.

21240259

M.B.Lazarus, Y.Nam, J.Jiang, P.Sliz, and S.Walker (2011).
Structure of human O-GlcNAc transferase and its complex with a peptide substrate.

Nature, 469, 564-567.

PDB codes:

3pe3 3pe4

21258330

T.M.Gloster, W.F.Zandberg, J.E.Heinonen, D.L.Shen, L.Deng, and D.J.Vocadlo (2011).
Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells.

Nat Chem Biol, 7, 174-181.

20661758

Y.Perez-Cervera, G.Harichaux, J.Schmidt, F.Debierre-Grockiego, V.Dehennaut, U.Bieker, E.Meurice, T.Lefebvre, and R.T.Schwarz (2011).
Direct evidence of O-GlcNAcylation in the apicomplexan Toxoplasma gondii: a biochemical and bioinformatic study.

Amino Acids, 40, 847-856.

19647786

C.Butkinaree, K.Park, and G.W.Hart (2010).
O-linked beta-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress.

Biochim Biophys Acta, 1800, 96.

19647043

J.A.Hanover, M.W.Krause, and D.C.Love (2010).
The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine.

Biochim Biophys Acta, 1800, 80-95.

21209858

K.J.Choi, S.Grass, S.Paek, J.W.St Geme, and H.J.Yeo (2010).
The Actinobacillus pleuropneumoniae HMW1C-like glycosyltransferase mediates N-linked glycosylation of the Haemophilus influenzae HMW1 adhesin.

PLoS One, 5, e15888.

19961900

N.E.Olszewski, C.M.West, S.O.Sassi, and L.M.Hartweck (2010).
O-GlcNAc protein modification in plants: Evolution and function.

Biochim Biophys Acta, 1800, 49-56.

20396401

T.M.Gloster, and D.J.Vocadlo (2010).
Mechanism, Structure, and Inhibition of O-GlcNAc Processing Enzymes.

Curr Signal Transduct Ther, 5, 74-91.

19028792

B.Laczy, B.G.Hill, K.Wang, A.J.Paterson, C.R.White, D.Xing, Y.F.Chen, V.Darley-Usmar, S.Oparil, and J.C.Chatham (2009).
Protein O-GlcNAcylation: a new signaling paradigm for the cardiovascular system.

Am J Physiol Heart Circ Physiol, 296, H13-H28.

19666537

D.A.Sinclair, M.Syrzycka, M.S.Macauley, T.Rastgardani, I.Komljenovic, D.J.Vocadlo, H.W.Brock, and B.M.Honda (2009).
Drosophila O-GlcNAc transferase (OGT) is encoded by the Polycomb group (PcG) gene, super sex combs (sxc).

Proc Natl Acad Sci U S A, 106, 13427-13432.

19383152

D.M.Webster, C.F.Teo, Y.Sun, D.Wloga, S.Gay, K.D.Klonowski, L.Wells, and S.T.Dougan (2009).
O-GlcNAc modifications regulate cell survival and epiboly during zebrafish development.

BMC Dev Biol, 9, 28.

19478141

M.C.Gambetta, K.Oktaba, and J.Müller (2009).
Essential role of the glycosyltransferase sxc/Ogt in polycomb repression.

Science, 325, 93-96.

18948359

S.Banerjee, P.W.Robbins, and J.Samuelson (2009).
Molecular characterization of nucleocytosolic O-GlcNAc transferases of Giardia lamblia and Cryptosporidium parvum.

Glycobiology, 19, 331-336.

18822375

B.Henrissat, G.Sulzenbacher, and Y.Bourne (2008).
Glycosyltransferases, glycoside hydrolases: surprise, surprise!

Curr Opin Struct Biol, 18, 527-533.

18822376

R.Hurtado-Guerrero, H.C.Dorfmueller, and D.M.van Aalten (2008).
Molecular mechanisms of O-GlcNAcylation.

Curr Opin Struct Biol, 18, 551-557.

18840611

W.D.Cheung, K.Sakabe, M.P.Housley, W.B.Dias, and G.W.Hart (2008).
O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins.

J Biol Chem, 283, 33935-33941.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.