2b61

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[[Image:2b61.gif|left|200px]]
[[Image:2b61.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2b61 |SIZE=350|CAPTION= <scene name='initialview01'>2b61</scene>, resolution 1.650&Aring;
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The line below this paragraph, containing "STRUCTURE_2b61", creates the "Structure Box" on the page.
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|SITE=
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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=MSE:SELENOMETHIONINE'>MSE</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/Homoserine_O-acetyltransferase Homoserine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.31 2.3.1.31] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= metX, met2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae])
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|DOMAIN=
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{{STRUCTURE_2b61| PDB=2b61 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b61 OCA], [http://www.ebi.ac.uk/pdbsum/2b61 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b61 RCSB]</span>
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'''Crystal Structure of Homoserine Transacetylase'''
'''Crystal Structure of Homoserine Transacetylase'''
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Revision as of 16:54, 3 May 2008

Image:2b61.gif

Template:STRUCTURE 2b61

Crystal Structure of Homoserine Transacetylase


Overview

Homoserine transacetylase catalyzes one of the required steps in the biosynthesis of methionine in fungi and several bacteria. We have determined the crystal structure of homoserine transacetylase from Haemophilus influenzae to a resolution of 1.65 A. The structure identifies this enzyme to be a member of the alpha/beta-hydrolase structural superfamily. The active site of the enzyme is located near the end of a deep tunnel formed by the juxtaposition of two domains and incorporates a catalytic triad involving Ser143, His337, and Asp304. A structural basis is given for the observed double displacement kinetic mechanism of homoserine transacetylase. Furthermore, the properties of the tunnel provide a rationale for how homoserine transacetylase catalyzes a transferase reaction vs hydrolysis, despite extensive similarity in active site architecture to hydrolytic enzymes.

About this Structure

2B61 is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.

Reference

Crystal structure of homoserine transacetylase from Haemophilus influenzae reveals a new family of alpha/beta-hydrolases., Mirza IA, Nazi I, Korczynska M, Wright GD, Berghuis AM, Biochemistry. 2005 Dec 6;44(48):15768-73. PMID:16313180 Page seeded by OCA on Sat May 3 19:54:05 2008

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