2b61

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[[Image:2b61.gif|left|200px]]<br /><applet load="2b61" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2b61.gif|left|200px]]
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caption="2b61, resolution 1.650&Aring;" />
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'''Crystal Structure of Homoserine Transacetylase'''<br />
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{{Structure
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|PDB= 2b61 |SIZE=350|CAPTION= <scene name='initialview01'>2b61</scene>, resolution 1.650&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [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]
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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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}}
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'''Crystal Structure of Homoserine Transacetylase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2B61 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B61 OCA].
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2B61 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B61 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16313180 16313180]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16313180 16313180]
[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
[[Category: Homoserine O-acetyltransferase]]
[[Category: Homoserine O-acetyltransferase]]
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[[Category: alpha-beta hydrolase fold]]
[[Category: alpha-beta hydrolase fold]]
[[Category: aspartate pathway]]
[[Category: aspartate pathway]]
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[[Category: coenzyme a]]
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[[Category: coenzyme some]]
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[[Category: structure-function studies]]
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[[Category: structure-function study]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:34:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:58:02 2008''

Revision as of 13:58, 20 March 2008


PDB ID 2b61

Drag the structure with the mouse to rotate
, resolution 1.650Å
Gene: metX, met2 (Haemophilus influenzae)
Activity: Homoserine O-acetyltransferase, with EC number 2.3.1.31
Coordinates: save as pdb, mmCIF, xml



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

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