2v03

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[[Image:2v03.jpg|left|200px]]
[[Image:2v03.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2v03 |SIZE=350|CAPTION= <scene name='initialview01'>2v03</scene>, resolution 1.33&Aring;
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The line below this paragraph, containing "STRUCTURE_2v03", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Gol+Binding+Site+For+Chain+A'>AC2</scene> and <scene name='pdbsite=AC3:Cit+Binding+Site+For+Chain+A'>AC3</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine_synthase Cysteine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.47 2.5.1.47] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_2v03| PDB=2v03 | SCENE= }}
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|RELATEDENTRY=[[2bhs|2BHS]], [[2bht|2BHT]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v03 OCA], [http://www.ebi.ac.uk/pdbsum/2v03 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v03 RCSB]</span>
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}}
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'''HIGH RESOLUTION STRUCTURE AND CATALYSIS OF AN O-ACETYLSERINE SULFHYDRYLASE'''
'''HIGH RESOLUTION STRUCTURE AND CATALYSIS OF AN O-ACETYLSERINE SULFHYDRYLASE'''
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[[Category: Wiesand, U.]]
[[Category: Wiesand, U.]]
[[Category: Zocher, G.]]
[[Category: Zocher, G.]]
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[[Category: amino-acid biosynthesis]]
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[[Category: Amino-acid biosynthesis]]
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[[Category: cysteine biosynthesis]]
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[[Category: Cysteine biosynthesis]]
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[[Category: enzymatic sythesis of novel compound]]
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[[Category: Enzymatic sythesis of novel compound]]
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[[Category: enzyme kinetic]]
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[[Category: Enzyme kinetic]]
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[[Category: pyridoxal phosphate]]
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[[Category: Pyridoxal phosphate]]
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[[Category: transferase]]
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[[Category: Transferase]]
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[[Category: x-ray diffraction]]
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[[Category: X-ray diffraction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:56:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:06:53 2008''
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Revision as of 14:56, 4 May 2008

Image:2v03.jpg

Template:STRUCTURE 2v03

HIGH RESOLUTION STRUCTURE AND CATALYSIS OF AN O-ACETYLSERINE SULFHYDRYLASE


Overview

The crystal structure of the dimeric O-acetylserine sulfhydrylase isozyme B from Escherichia coli (CysM), complexed with the substrate analog citrate, has been determined at 1.33 A resolution by X-ray diffraction analysis. The C1-carboxylate of citrate was bound at the carboxylate position of O-acetylserine, whereas the C6-carboxylate adopted two conformations. The activity of the enzyme and of several active center mutants was determined using an assay based on O-acetylserine and thio-nitrobenzoate (TNB). The unnatural substrate TNB was modeled into the reported structure. The substrate model and the observed mutant activities may facilitate future protein engineering attempts designed to broaden the substrate spectrum of the enzyme. A comparison of the reported structure with previously published CysM structures revealed large conformational changes. One of the crystal forms contained two dimers, each of which comprised one subunit in a closed and one in an open conformation. Although the homodimer asymmetry was most probably caused by crystal packing, it indicates that the enzyme can adopt such a state in solution, which may be relevant for the catalytic reaction.

About this Structure

2V03 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

High resolution structure and catalysis of O-acetylserine sulfhydrylase isozyme B from Escherichia coli., Zocher G, Wiesand U, Schulz GE, FEBS J. 2007 Oct;274(20):5382-9. Epub 2007 Sep 26. PMID:17894825 Page seeded by OCA on Sun May 4 17:56:36 2008

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OCA

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