1mpx
From Proteopedia
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|PDB= 1mpx |SIZE=350|CAPTION= <scene name='initialview01'>1mpx</scene>, resolution 1.90Å | |PDB= 1mpx |SIZE=350|CAPTION= <scene name='initialview01'>1mpx</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-amino-acid_esterase Alpha-amino-acid esterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.43 3.1.1.43] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-amino-acid_esterase Alpha-amino-acid esterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.43 3.1.1.43] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mpx OCA], [http://www.ebi.ac.uk/pdbsum/1mpx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mpx RCSB]</span> | ||
}} | }} | ||
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[[Category: Polderman-Tijmes, J J.]] | [[Category: Polderman-Tijmes, J J.]] | ||
[[Category: Vries, E J.de.]] | [[Category: Vries, E J.de.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: GOL]] | ||
[[Category: alpha/beta hydrolase]] | [[Category: alpha/beta hydrolase]] | ||
[[Category: jellyroll]] | [[Category: jellyroll]] | ||
[[Category: selenomethionine]] | [[Category: selenomethionine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:19:27 2008'' |
Revision as of 19:19, 30 March 2008
| |||||||
| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Alpha-amino-acid esterase, with EC number 3.1.1.43 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ALPHA-AMINO ACID ESTER HYDROLASE LABELED WITH SELENOMETHIONINE
Overview
alpha-Amino acid ester hydrolases (AEHs) catalyze the hydrolysis and synthesis of esters and amides with an alpha-amino group. As such, they can synthesize beta-lactam antibiotics from acyl compounds and beta-lactam nuclei obtained from the hydrolysis of natural antibiotics. This article describes the gene sequence and the 1.9-A resolution crystal structure of the AEH from Xanthomonas citri. The enzyme consists of an alpha/beta-hydrolase fold domain, a helical cap domain, and a jellyroll beta-domain. Structural homology was observed to the Rhodococcus cocaine esterase, indicating that both enzymes belong to the same class of bacterial hydrolases. Docking of a beta-lactam antibiotic in the active site explains the substrate specificity, specifically the necessity of an alpha-amino group on the substrate, and explains the low specificity toward the beta-lactam nucleus.
About this Structure
1MPX is a Single protein structure of sequence from Xanthomonas citri. Full crystallographic information is available from OCA.
Reference
The sequence and crystal structure of the alpha-amino acid ester hydrolase from Xanthomonas citri define a new family of beta-lactam antibiotic acylases., Barends TR, Polderman-Tijmes JJ, Jekel PA, Hensgens CM, de Vries EJ, Janssen DB, Dijkstra BW, J Biol Chem. 2003 Jun 20;278(25):23076-84. Epub 2003 Apr 8. PMID:12684501
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