2bmi
From Proteopedia
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[[Image:2bmi.jpg|left|200px]] | [[Image:2bmi.jpg|left|200px]] | ||
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'''METALLO-BETA-LACTAMASE''' | '''METALLO-BETA-LACTAMASE''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BMI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteroides_fragilis Bacteroides fragilis]. This structure supersedes the now removed PDB entry | + | 2BMI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteroides_fragilis Bacteroides fragilis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1bmi 1bmi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BMI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Dideberg, O.]] | [[Category: Dideberg, O.]] | ||
[[Category: Duee, E.]] | [[Category: Duee, E.]] | ||
| - | [[Category: | + | [[Category: Beta-lactamase]] |
| - | [[Category: | + | [[Category: Metallo beta-lactamase]] |
| - | [[Category: | + | [[Category: Zinc]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:29:57 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:29, 3 May 2008
METALLO-BETA-LACTAMASE
Overview
beta-Lactamases are extracellular or periplasmic bacterial enzymes which confer resistance to beta-lactam antibiotics. On the basis of their catalytic mechanisms, they can be divided into two major groups: active-site serine enzymes (classes A, C and D) and the ZnII enzymes (class B). The first crystal structure of a class B enzyme, the metallo-beta-lactamase from Bacillus cereus, has been solved at 2.5 A resolution [Carfi, Pares, Duee, Galleni, Duez, Frere & Dideberg (1995). EMBO J. 14, 4914-4921]. Recently, the crystal structure of the metallo-beta-lactamase from Bacteroides fragilis has been determined in a tetragonal space group [Concha, Rasmussen, Bush & Herzberg (1996). Structure, 4, 823-836]. The structure of the metallo-beta-lactamase from B. fragilis in an orthorhombic crystal form at 2.0 A resolution is reported here. The final crystallographic R is 0.196 for all the 32501 observed reflections in the range 10-2.0 A. The refined model includes 458 residues, 437 water molecules, four zinc and two sodium ions. These structures are discussed with reference to Zn binding and activity. A catalytic mechanism is proposed which is coherent with metallo-beta-lactamases being active with either one Zn ion (as in Aeromonas hydrophila) or two Zn ions (as in B. fragilis) bound to the protein.
About this Structure
2BMI is a Single protein structure of sequence from Bacteroides fragilis. This structure supersedes the now removed PDB entry 1bmi. Full crystallographic information is available from OCA.
Reference
X-ray structure of the ZnII beta-lactamase from Bacteroides fragilis in an orthorhombic crystal form., Carfi A, Duee E, Paul-Soto R, Galleni M, Frere JM, Dideberg O, Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):45-57. PMID:9761816 Page seeded by OCA on Sat May 3 20:29:57 2008
