2bg7: Difference between revisions
New page: left|200px<br /> <applet load="2bg7" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bg7, resolution 2.1Å" /> '''BACILLUS CEREUS META... |
No edit summary |
||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
2BG7 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]] with ZN, SO4 and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. 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=2BG7 OCA]]. | 2BG7 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]] with ZN, SO4 and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Hydrolase Hydrolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BG7 OCA]]. | ||
==Reference== | ==Reference== | ||
| Line 27: | Line 27: | ||
[[Category: zinc]] | [[Category: zinc]] | ||
''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 08:45:33 2007'' | ||
Revision as of 09:40, 30 October 2007
|
BACILLUS CEREUS METALLO-BETA-LACTAMASE (BCII) ARG (121) CYS MUTANT. SOLVED AT PH4.5 USING 20 MICROMOLAR ZNSO4 IN THE BUFFER. 1MM DTT WAS USED AS A REDUCING AGENT. CYS221 IS OXIDIZED.
OverviewOverview
The zinc-dependent metallo-beta-lactamases are a group of bacterial, enzymes that pose a threat to the future efficacy of present-day, antibiotics. Their mechanism is poorly understood, and there are no, clinically useful inhibitors. While most members of the group contain two, tightly bound zinc ions in their active sites, the Bacillus cereus enzyme, has a much lower affinity for its second zinc (Zn2), thought to be due to, the presence of Arg121 immediately beneath the floor of the active site, (cf. Cys/Ser/His121 in the bizinc enzymes). Crystal structures of the, Arg121Cys mutant of the B. cereus 569/H/9 enzyme were solved at pH 7.0, 5.0, and 4.5, each in the presence of either 20 microM or 20 mM Zn(2+) to, generate the mono- and bizinc forms, respectively. Surprisingly, the, structure ... [(full description)]
About this StructureAbout this Structure
2BG7 is a [Single protein] structure of sequence from [Bacillus cereus] with ZN, SO4 and GOL as [ligands]. Active as [Hydrolase], with EC number [3.5.2.6]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Effect of pH on the active site of an Arg121Cys mutant of the metallo-beta-lactamase from Bacillus cereus: implications for the enzyme mechanism., Davies AM, Rasia RM, Vila AJ, Sutton BJ, Fabiane SM, Biochemistry. 2005 Mar 29;44(12):4841-9. PMID:15779910
Page seeded by OCA on Tue Oct 30 08:45:33 2007