1mpx
From Proteopedia
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| - | [[Image:1mpx.gif|left|200px]] | + | [[Image:1mpx.gif|left|200px]] |
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| - | '''ALPHA-AMINO ACID ESTER HYDROLASE LABELED WITH SELENOMETHIONINE''' | + | {{Structure |
| + | |PDB= 1mpx |SIZE=350|CAPTION= <scene name='initialview01'>1mpx</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ALPHA-AMINO ACID ESTER HYDROLASE LABELED WITH SELENOMETHIONINE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MPX is a [ | + | 1MPX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_citri Xanthomonas citri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MPX OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12684501 12684501] |
[[Category: Alpha-amino-acid esterase]] | [[Category: Alpha-amino-acid esterase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: selenomethionine]] | [[Category: selenomethionine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:46:39 2008'' |
Revision as of 10:46, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Ligands: | and | ||||||
| Activity: | Alpha-amino-acid esterase, with EC number 3.1.1.43 | ||||||
| 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
Page seeded by OCA on Thu Mar 20 12:46:39 2008
