2b61
From Proteopedia
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|PDB= 2b61 |SIZE=350|CAPTION= <scene name='initialview01'>2b61</scene>, resolution 1.650Å | |PDB= 2b61 |SIZE=350|CAPTION= <scene name='initialview01'>2b61</scene>, resolution 1.650Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
| - | |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] | + | |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> |
|GENE= metX, met2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae]) | |GENE= metX, met2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: structure-function study]] | [[Category: structure-function study]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:01:59 2008'' |
Revision as of 23:02, 30 March 2008
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| , resolution 1.650Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | metX, met2 (Haemophilus influenzae) | ||||||
| Activity: | Homoserine O-acetyltransferase, with EC number 2.3.1.31 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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