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1mpx
From Proteopedia
(New page: 200px<br /><applet load="1mpx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mpx, resolution 1.90Å" /> '''ALPHA-AMINO ACID EST...) |
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| - | [[Image:1mpx.gif|left|200px]]<br /><applet load="1mpx" size=" | + | [[Image:1mpx.gif|left|200px]]<br /><applet load="1mpx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mpx, resolution 1.90Å" /> | caption="1mpx, resolution 1.90Å" /> | ||
'''ALPHA-AMINO ACID ESTER HYDROLASE LABELED WITH SELENOMETHIONINE'''<br /> | '''ALPHA-AMINO ACID ESTER HYDROLASE LABELED WITH SELENOMETHIONINE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | alpha-Amino acid ester hydrolases (AEHs) catalyze the hydrolysis and | + | 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== | ==About this Structure== | ||
| - | 1MPX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_citri Xanthomonas citri] with CA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1MPX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_citri Xanthomonas citri] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MPX OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xanthomonas citri]] | [[Category: Xanthomonas citri]] | ||
| - | [[Category: Barends, T | + | [[Category: Barends, T R.M.]] |
| - | [[Category: Dijkstra, B | + | [[Category: Dijkstra, B W.]] |
| - | [[Category: Hensgens, C | + | [[Category: Hensgens, C M.H.]] |
| - | [[Category: Janssen, D | + | [[Category: Janssen, D B.]] |
| - | [[Category: Jekel, P | + | [[Category: Jekel, P A.]] |
| - | [[Category: Polderman-Tijmes, J | + | [[Category: Polderman-Tijmes, J J.]] |
| - | [[Category: Vries, E | + | [[Category: Vries, E J.de.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
| Line 27: | Line 27: | ||
[[Category: selenomethionine]] | [[Category: selenomethionine]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:56 2008'' |
Revision as of 11:57, 21 February 2008
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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 with and as ligands. Active as Alpha-amino-acid esterase, with EC number 3.1.1.43 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 Feb 21 13:57:56 2008
