2fu8: Difference between revisions

Revision as of 04:18, 4 May 2008

Zinc-beta-lactamase L1 from stenotrophomonas maltophilia (d-captopril complex)

OverviewOverview

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 StructureAbout this Structure

2FU8 is a Single protein structure of sequence from Stenotrophomonas maltophilia. Full crystallographic information is available from OCA.

ReferenceReference

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 Sun May 4 04:18:54 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 [[Image:2fu8.jpg|left|200px]]
- {{Structure
+<!--
-|PDB= 2fu8 |SIZE=350|CAPTION= <scene name='initialview01'>2fu8</scene>, resolution 1.80&Aring;
+The line below this paragraph, containing "STRUCTURE_2fu8", creates the "Structure Box" on the page.
-|SITE=
+You may change the PDB parameter (which sets the PDB file loaded into the applet)
-|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MCO:1-(3-MERCAPTO-2-METHYL-PROPIONYL)-PYRROLIDINE-2-CARBOXYLIC+ACID'>MCO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
+or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-|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>
+or leave the SCENE parameter empty for the default display.
-|GENE= L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=40324 Stenotrophomonas maltophilia])
+-->
-|DOMAIN=
+{{STRUCTURE_2fu8|  PDB=2fu8  |  SCENE=  }}
-|RELATEDENTRY=[[2fm6|2FM6]], [[2fu6|2FU6]], [[2fu7|2FU7]], [[2fu9|2FU9]]
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fu8 OCA], [http://www.ebi.ac.uk/pdbsum/2fu8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fu8 RCSB]</span>
-}}
 '''Zinc-beta-lactamase L1 from stenotrophomonas maltophilia (d-captopril complex)'''
@@ Line 30: / Line 27: @@
 [[Category: Kahn, R.]]
 [[Category: Nauton, L.]]
-[[Category: hydrolase]]
+[[Category: Hydrolase]]
-[[Category: inhibitor]]
+[[Category: Inhibitor]]
-[[Category: lactamase]]
+[[Category: Lactamase]]
-[[Category: metallo]]
+[[Category: Metallo]]
-[[Category: zn]]
+[[Category: Zn]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:18:54 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:07:48 2008''