1vm1

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(New page: 200px<br /><applet load="1vm1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vm1, resolution 2.02&Aring;" /> '''STRUCTURE OF SHV-1 B...)
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[[Image:1vm1.gif|left|200px]]<br /><applet load="1vm1" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1vm1, resolution 2.02&Aring;" />
caption="1vm1, resolution 2.02&Aring;" />
'''STRUCTURE OF SHV-1 BETA-LACTAMASE INHIBITED BY TAZOBACTAM'''<br />
'''STRUCTURE OF SHV-1 BETA-LACTAMASE INHIBITED BY TAZOBACTAM'''<br />
==Overview==
==Overview==
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Two species resulting from the reaction of the SHV-1 class A, beta-lactamase with the sulfone inhibitor tazobactam have been trapped at, 100 K and mapped by X-ray crystallography at 2.0 A resolution. An acyclic, form of tazobactam is covalently bonded to the catalytic Ser70 side chain, and a second species, a five-atom vinyl carboxylic acid fragment of, tazobactam, is bonded to Ser130. It is proposed that the electron density, map of the crystal is a composite picture of two complexes, each with only, a single bound species. It is estimated that the two complexes exist in, the crystal in approximately equal populations. Results are discussed in, relation to the mechanism-based inhibition of class A beta-lactamases by, the similar inhibitors sulbactam and clavulanic acid.
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Two species resulting from the reaction of the SHV-1 class A beta-lactamase with the sulfone inhibitor tazobactam have been trapped at 100 K and mapped by X-ray crystallography at 2.0 A resolution. An acyclic form of tazobactam is covalently bonded to the catalytic Ser70 side chain, and a second species, a five-atom vinyl carboxylic acid fragment of tazobactam, is bonded to Ser130. It is proposed that the electron density map of the crystal is a composite picture of two complexes, each with only a single bound species. It is estimated that the two complexes exist in the crystal in approximately equal populations. Results are discussed in relation to the mechanism-based inhibition of class A beta-lactamases by the similar inhibitors sulbactam and clavulanic acid.
==About this Structure==
==About this Structure==
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1VM1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae] with MA4, TBE, AKR and TAZ as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1G56. Active as [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VM1 OCA].
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1VM1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae] with <scene name='pdbligand=MA4:'>MA4</scene>, <scene name='pdbligand=TBE:'>TBE</scene>, <scene name='pdbligand=AKR:'>AKR</scene> and <scene name='pdbligand=TAZ:'>TAZ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1G56. Active as [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VM1 OCA].
==Reference==
==Reference==
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[[Category: Klebsiella pneumoniae]]
[[Category: Klebsiella pneumoniae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bonomo, R.A.]]
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[[Category: Bonomo, R A.]]
[[Category: Hujer, A.]]
[[Category: Hujer, A.]]
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[[Category: Knox, J.R.]]
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[[Category: Knox, J R.]]
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[[Category: Kuzin, A.P.]]
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[[Category: Kuzin, A P.]]
[[Category: Nukaga, M.]]
[[Category: Nukaga, M.]]
[[Category: Nukaga, Y.]]
[[Category: Nukaga, Y.]]
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[[Category: penicillinase]]
[[Category: penicillinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:49:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:36:40 2008''

Revision as of 13:36, 21 February 2008


1vm1, resolution 2.02Å

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STRUCTURE OF SHV-1 BETA-LACTAMASE INHIBITED BY TAZOBACTAM

Overview

Two species resulting from the reaction of the SHV-1 class A beta-lactamase with the sulfone inhibitor tazobactam have been trapped at 100 K and mapped by X-ray crystallography at 2.0 A resolution. An acyclic form of tazobactam is covalently bonded to the catalytic Ser70 side chain, and a second species, a five-atom vinyl carboxylic acid fragment of tazobactam, is bonded to Ser130. It is proposed that the electron density map of the crystal is a composite picture of two complexes, each with only a single bound species. It is estimated that the two complexes exist in the crystal in approximately equal populations. Results are discussed in relation to the mechanism-based inhibition of class A beta-lactamases by the similar inhibitors sulbactam and clavulanic acid.

About this Structure

1VM1 is a Single protein structure of sequence from Klebsiella pneumoniae with , , and as ligands. This structure supersedes the now removed PDB entry 1G56. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.

Reference

Inhibition of the SHV-1 beta-lactamase by sulfones: crystallographic observation of two reaction intermediates with tazobactam., Kuzin AP, Nukaga M, Nukaga Y, Hujer A, Bonomo RA, Knox JR, Biochemistry. 2001 Feb 13;40(6):1861-6. PMID:11327849

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