1gvg

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[[Image:1gvg.jpg|left|200px]]
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{{STRUCTURE_1gvg| PDB=1gvg | SCENE= }}
{{STRUCTURE_1gvg| PDB=1gvg | SCENE= }}
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'''CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE WITH NITRIC OXIDE'''
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===CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE WITH NITRIC OXIDE===
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==Overview==
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Clavaminate synthase (CAS), a 2-oxoglutarate (2OG) dependent dioxygenase, catalyses three steps in the biosynthesis of clavulanic acid. Crystals of CAS complexed with Fe(II), 2OG and deoxyguanidinoproclavaminate were exposed to nitric oxide (NO) acting as a dioxygen analogue. Prior to exposure with NO, the active site Fe(II) is octahedrally coordinated by a water molecule, the 2-oxo and 1-carboxylate groups of 2OG, and the side-chains of an aspartyl and two histidinyl residues. NO binds to the position previously occupied by the 2OG 1-carboxylate concomitant with rearrangement of the latter to the position previously occupied by the displaced water.
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The line below this paragraph, {{ABSTRACT_PUBMED_12062399}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 12062399 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12062399}}
==About this Structure==
==About this Structure==
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[[Category: Oxygenase]]
[[Category: Oxygenase]]
[[Category: Trifunctional enzyme]]
[[Category: Trifunctional enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:03:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:08:50 2008''

Revision as of 03:08, 1 July 2008

Template:STRUCTURE 1gvg

CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE WITH NITRIC OXIDE

Template:ABSTRACT PUBMED 12062399

About this Structure

1GVG is a Single protein structure of sequence from Streptomyces clavuligerus. Full crystallographic information is available from OCA.

Reference

Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate-substrate-NO complex: evidence for metal centered rearrangements., Zhang Z, Ren J, Harlos K, McKinnon CH, Clifton IJ, Schofield CJ, FEBS Lett. 2002 Apr 24;517(1-3):7-12. PMID:12062399

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