2bls: Difference between revisions
New page: left|200px<br /> <applet load="2bls" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bls, resolution 2.0Å" /> '''AMPC BETA-LACTAMASE ... |
No edit summary |
||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
2BLS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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=2BLS OCA]]. | 2BLS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]]. 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]]. Structure known Active Sites: ACB and ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BLS OCA]]. | ||
==Reference== | ==Reference== | ||
Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design., Usher KC, Blaszczak LC, Weston GS, Shoichet BK, Remington SJ, Biochemistry. 1998 Nov 17;37(46):16082-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9819201 9819201] | Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design., Usher KC, Blaszczak LC, Weston GS, Shoichet BK, Remington SJ, Biochemistry. 1998 Nov 17;37(46):16082-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9819201 9819201] | ||
[[Category: Beta-lactamase]] | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 22: | Line 23: | ||
[[Category: serine hydrolase]] | [[Category: serine hydrolase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:52:06 2007'' | ||
Revision as of 11:47, 30 October 2007
|
AMPC BETA-LACTAMASE FROM ESCHERICHIA COLI
Overview
The structures of AmpC beta-lactamase from Escherichia coli, alone and in, complex with a transition-state analogue, have been determined by X-ray, crystallography. The native enzyme was determined to 2.0 A resolution, and, the structure with the transition-state analogue m-aminophenylboronic acid, was determined to 2.3 A resolution. The structure of AmpC from E. coli, resembles those previously determined for the class C enzymes from, Enterobacter cloacae and Citrobacter freundii. The transition-state, analogue, m-aminophenylboronic acid, makes several interactions with AmpC, that were unexpected. Perhaps most surprisingly, the putative "oxyanion", of the boronic acid forms what appears to be a hydrogen bond with the, backbone carbonyl oxygen of Ala318, suggesting that this atom is, ... [(full description)]
About this Structure
2BLS is a [Single protein] structure of sequence from [Escherichia coli]. Active as [Beta-lactamase], with EC number [3.5.2.6]. Structure known Active Sites: ACB and ACT. Full crystallographic information is available from [OCA].
Reference
Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design., Usher KC, Blaszczak LC, Weston GS, Shoichet BK, Remington SJ, Biochemistry. 1998 Nov 17;37(46):16082-92. PMID:9819201
Page seeded by OCA on Tue Oct 30 13:52:06 2007
