1gvg

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[[Image:1gvg.jpg|left|200px]]<br /><applet load="1gvg" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gvg.jpg|left|200px]]
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caption="1gvg, resolution 1.54&Aring;" />
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'''CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE WITH NITRIC OXIDE'''<br />
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{{Structure
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|PDB= 1gvg |SIZE=350|CAPTION= <scene name='initialview01'>1gvg</scene>, resolution 1.54&Aring;
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|SITE= <scene name='pdbsite=AC1:Nmo+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=NO:NITROGEN+OXIDE'>NO</scene>, <scene name='pdbligand=AKG:2-OXYGLUTARIC+ACID'>AKG</scene> and <scene name='pdbligand=PCX:DEOXYGUANIDINOPROCLAVAMINIC ACID'>PCX</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE WITH NITRIC OXIDE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1GVG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=NO:'>NO</scene>, <scene name='pdbligand=AKG:'>AKG</scene> and <scene name='pdbligand=PCX:'>PCX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Nmo+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GVG OCA].
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1GVG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GVG OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12062399 12062399]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12062399 12062399]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptomyces clavuligerus]]
[[Category: Streptomyces clavuligerus]]
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[[Category: trifunctional enzyme]]
[[Category: trifunctional enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:54:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:28:27 2008''

Revision as of 09:28, 20 March 2008


PDB ID 1gvg

Drag the structure with the mouse to rotate
, resolution 1.54Å
Sites:
Ligands: , , , and
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE WITH NITRIC OXIDE


Overview

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.

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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