1bmc

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[[Image:1bmc.gif|left|200px]]
[[Image:1bmc.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1bmc |SIZE=350|CAPTION= <scene name='initialview01'>1bmc</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1bmc", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=ZN:Zn+Binding+Site'>ZN</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1bmc| PDB=1bmc | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bmc OCA], [http://www.ebi.ac.uk/pdbsum/1bmc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bmc RCSB]</span>
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}}
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'''STRUCTURE OF A ZINC METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS'''
'''STRUCTURE OF A ZINC METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS'''
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[[Category: Duee, E.]]
[[Category: Duee, E.]]
[[Category: Pares, S.]]
[[Category: Pares, S.]]
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[[Category: antibiotic resistance]]
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[[Category: Antibiotic resistance]]
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[[Category: hydrolase (acting in cyclic amides)]]
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[[Category: Signal]]
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[[Category: signal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:41:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:03:53 2008''
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Revision as of 08:41, 2 May 2008

Image:1bmc.gif

Template:STRUCTURE 1bmc

STRUCTURE OF A ZINC METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS


Overview

The 3-D structure of Bacillus cereus (569/H/9) beta-lactamase (EC 3.5.2.6), which catalyses the hydrolysis of nearly all beta-lactams, has been solved at 2.5 A resolution by the multiple isomorphous replacement method, with density modification and phase combination, from crystals of the native protein and of a specially designed mutant (T97C). The current model includes 212 of the 227 amino acid residues, the zinc ion and 10 water molecules. The protein is folded into a beta beta sandwich with helices on each external face. To our knowledge, this fold has never been observed. An approximate internal molecular symmetry is found, with a 2-fold axis passing roughly through the zinc ion and suggesting a possible gene duplication. The active site is located at one edge of the beta beta sandwich and near the N-terminal end of a helix. The zinc ion is coordinated by three histidine residues (86, 88 and 149) and a water molecule. A sequence comparison of the relevant metallo-beta-lactamases, based on this protein structure, highlights a few well-conserved amino acid residues. The structure shows that most of these residues are in the active site. Among these, aspartic acid 90 and histidine 210 participate in a proposed catalytic mechanism for beta-lactam hydrolysis.

About this Structure

1BMC is a Single protein structure of sequence from Bacillus cereus. Full crystallographic information is available from OCA.

Reference

The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold., Carfi A, Pares S, Duee E, Galleni M, Duez C, Frere JM, Dideberg O, EMBO J. 1995 Oct 16;14(20):4914-21. PMID:7588620 Page seeded by OCA on Fri May 2 11:41:52 2008

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