1mpx

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(New page: 200px<br /><applet load="1mpx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mpx, resolution 1.90&Aring;" /> '''ALPHA-AMINO ACID EST...)
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[[Image:1mpx.gif|left|200px]]<br /><applet load="1mpx" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1mpx.gif|left|200px]]<br /><applet load="1mpx" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mpx, resolution 1.90&Aring;" />
caption="1mpx, resolution 1.90&Aring;" />
'''ALPHA-AMINO ACID ESTER HYDROLASE LABELED WITH SELENOMETHIONINE'''<br />
'''ALPHA-AMINO ACID ESTER HYDROLASE LABELED WITH SELENOMETHIONINE'''<br />
==Overview==
==Overview==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MPX OCA].
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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==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Xanthomonas citri]]
[[Category: Xanthomonas citri]]
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[[Category: Barends, T.R.M.]]
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[[Category: Barends, T R.M.]]
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[[Category: Dijkstra, B.W.]]
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[[Category: Dijkstra, B W.]]
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[[Category: Hensgens, C.M.H.]]
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[[Category: Hensgens, C M.H.]]
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[[Category: Janssen, D.B.]]
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[[Category: Janssen, D B.]]
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[[Category: Jekel, P.A.]]
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[[Category: Jekel, P A.]]
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[[Category: Polderman-Tijmes, J.J.]]
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[[Category: Polderman-Tijmes, J J.]]
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[[Category: Vries, E.J.de.]]
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[[Category: Vries, E J.de.]]
[[Category: CA]]
[[Category: CA]]
[[Category: GOL]]
[[Category: GOL]]
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[[Category: selenomethionine]]
[[Category: selenomethionine]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 21:48:44 2007''
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''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


1mpx, resolution 1.90Å

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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

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