1vz8
From Proteopedia
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|PDB= 1vz8 |SIZE=350|CAPTION= <scene name='initialview01'>1vz8</scene>, resolution 2.75Å | |PDB= 1vz8 |SIZE=350|CAPTION= <scene name='initialview01'>1vz8</scene>, resolution 2.75Å | ||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Glutamate_N-acetyltransferase Glutamate N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.35 2.3.1.35] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_N-acetyltransferase Glutamate N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.35 2.3.1.35] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vz8 OCA], [http://www.ebi.ac.uk/pdbsum/1vz8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vz8 RCSB]</span> | ||
}} | }} | ||
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[[Category: Kershaw, N J.]] | [[Category: Kershaw, N J.]] | ||
[[Category: Schofield, C J.]] | [[Category: Schofield, C J.]] | ||
| - | [[Category: SO4]] | ||
[[Category: antibiotic]] | [[Category: antibiotic]] | ||
[[Category: clavulanic acid]] | [[Category: clavulanic acid]] | ||
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[[Category: ornithine acetyltransferase]] | [[Category: ornithine acetyltransferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:29:01 2008'' |
Revision as of 21:29, 30 March 2008
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| , resolution 2.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Glutamate N-acetyltransferase, with EC number 2.3.1.35 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ORNITHINE ACETYLTRANSFERASE (ORF6 GENE PRODUCT- CLAVULANIC ACID BIOSYNTHESIS) FROM STREPTOMYCES CLAVULIGERUS (SEMET STRUCTURE)
Overview
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.
About this Structure
1VZ8 is a Single protein structure of sequence from Streptomyces clavuligerus. Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of ornithine acetyltransferase from the clavulanic acid biosynthesis gene cluster., Elkins JM, Kershaw NJ, Schofield CJ, Biochem J. 2005 Jan 15;385(Pt 2):565-73. PMID:15352873
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