PDBsum entry 1vz7

Transferase

PDB id

1vz7

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Contents

			Protein chains

					376 a.a. *

			Ligands

					SO4 ×4

* Residue conservation analysis

PDB id:

1vz7

Links

Name:

Transferase

Title:

Ornithine acetyltransferase (orf6 gene product - clavulanic acid biosynthesis) from streptomyces clavuligerus

Structure:

Ornithine acetyl-transferase. Chain: a, b, c, d. Engineered: yes

Source:

Streptomyces clavuligerus. Organism_taxid: 1901. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Biol. unit:

Dimer (from PDB file)

Resolution:

3.00Å

R-factor:

0.223

R-free:

0.313

Authors:

J.M.Elkins,N.J.Kershaw,C.J.Schofield

Key ref:

J.M.Elkins et al. (2005). X-ray crystal structure of ornithine acetyltransferase from the clavulanic acid biosynthesis gene cluster. Biochem J, 385, 565-573. PubMed id: 15352873

Date:

14-May-04

Release date:

16-Sep-04

PROCHECK

	Headers

	References

Protein chains

P0DJQ5 (GNAT2_STRCL) - Glutamate N-acetyltransferase 2 from Streptomyces clavuligerus

Seq: Struc:					393 a.a. 376 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.2.3.1.35 - glutamate N-acetyltransferase.

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

Reaction:

N₂-acetyl-L-ornithine + L-glutamate = N-acetyl-L-glutamate + L-ornithine

N(2)-acetyl-L-ornithine	+	L-glutamate	=	N-acetyl-L-glutamate	+	L-ornithine

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

reference

	Biochem J 385:565-573 (2005)
PubMed id: 15352873

X-ray crystal structure of ornithine acetyltransferase from the clavulanic acid biosynthesis gene cluster.
J.M.Elkins, N.J.Kershaw, C.J.Schofield.

ABSTRACT

The orf6 gene from the clavulanic acid biosynthesis gene cluster encodes an OAT (ornithine acetyltransferase). Similar to other OATs the enzyme has been shown to catalyse the reversible transfer of an acetyl group from N-acetylornithine to glutamate. OATs are Ntn (N-terminal nucleophile) enzymes, but are distinct from the better-characterized Ntn hydrolase enzymes as they catalyse acetyl transfer rather than a hydrolysis reaction. In the present study, we describe the X-ray crystal structure of the OAT, corresponding to the orf6 gene product, to 2.8 A (1 A=0.1 nm) resolution. The larger domain of the structure consists of an alphabetabetaalpha sandwich as in the structures of Ntn hydrolase enzymes. However, differences in the connectivity reveal that OATs belong to a structural family different from that of other structurally characterized Ntn enzymes, with one exception: unexpectedly, the alphabetabetaalpha sandwich of ORF6 (where ORF stands for open reading frame) displays the same fold as an DmpA (L-aminopeptidase D-ala-esterase/amidase from Ochrobactrum anthropi), and so the OATs and DmpA form a new structural subfamily of Ntn enzymes. The structure reveals an alpha2beta2-heterotetrameric oligomerization state in which the intermolecular interface partly defines the active site. Models of the enzyme-substrate complexes suggest a probable oxyanion stabilization mechanism as well as providing insight into how the enzyme binds its two differently charged substrates.

Literature references that cite this PDB file's key reference

PubMed id

Reference

19194014

R.Sankaranarayanan, C.R.Garen, M.M.Cherney, M.Yuan, C.Lee, and M.N.James (2009).
Preliminary X-ray crystallographic analysis of ornithine acetyltransferase (Rv1653) from Mycobacterium tuberculosis.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 173-176.

17318535

B.Geueke, and H.P.Kohler (2007).
Bacterial beta-peptidyl aminopeptidases: on the hydrolytic degradation of beta-peptides.

Appl Microbiol Biotechnol, 74, 1197-1204.

17347518

Y.Xu, B.Labedan, and N.Glansdorff (2007).
Surprising arginine biosynthesis: a reappraisal of the enzymology and evolution of the pathway in microorganisms.

Microbiol Mol Biol Rev, 71, 36-47.

17142921

D.Maes, M.Crabeel, C.Van de Weerdt, J.Martial, E.Peeters, D.Charlier, K.Decanniere, C.Vanhee, L.Wyns, and I.Zegers (2006).
Crystallization of ornithine acetyltransferase from yeast by counter-diffusion and preliminary X-ray study.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 1294-1297.

16251194

H.Arulanantham, N.J.Kershaw, K.S.Hewitson, C.E.Hughes, J.E.Thirkettle, and C.J.Schofield (2006).
ORF17 from the clavulanic acid biosynthesis gene cluster catalyzes the ATP-dependent formation of N-glycyl-clavaminic acid.

J Biol Chem, 281, 279-287.

15937278

H.Cheng, and N.V.Grishin (2005).
DOM-fold: a structure with crossing loops found in DmpA, ornithine acetyltransferase, and molybdenum cofactor-binding domain.

Protein Sci, 14, 1902-1910.

15946951

K.Michalska, K.Brzezinski, and M.Jaskolski (2005).
Crystal structure of isoaspartyl aminopeptidase in complex with L-aspartate.

J Biol Chem, 280, 28484-28491.

PDB codes:

1seo 2zal

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.