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2fu9
From Proteopedia
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|PDB= 2fu9 |SIZE=350|CAPTION= <scene name='initialview01'>2fu9</scene>, resolution 1.80Å | |PDB= 2fu9 |SIZE=350|CAPTION= <scene name='initialview01'>2fu9</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MP2:N-[(BENZYLOXY)CARBONYL]-L-CYSTEINYLGLYCINE'>MP2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=40324 Stenotrophomonas maltophilia]) | |GENE= L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=40324 Stenotrophomonas maltophilia]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2fm6|2FM6]], [[2fu6|2FU6]], [[2fu7|2FU7]], [[2fu8|2FU8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fu9 OCA], [http://www.ebi.ac.uk/pdbsum/2fu9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fu9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Kahn, R.]] | [[Category: Kahn, R.]] | ||
[[Category: Nauton, L.]] | [[Category: Nauton, L.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: MP2]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: ZN]] | ||
[[Category: beta]] | [[Category: beta]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: zn]] | [[Category: zn]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:07:50 2008'' |
Revision as of 00:07, 31 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | L1 (Stenotrophomonas maltophilia) | ||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| Related: | 2FM6, 2FU6, 2FU7, 2FU8
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Zinc-beta-lactamase L1 from stenotrophomonas maltophilia (mp2 inhibitor complex)
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
2FU9 is a Single protein structure of sequence from Stenotrophomonas maltophilia. 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 Mon Mar 31 03:07:50 2008
Categories: Beta-lactamase | Single protein | Stenotrophomonas maltophilia | Dideberg, O. | Garau, G. | Kahn, R. | Nauton, L. | Beta | Hydrolase | Inhibitor | Lactamase | Metallo | Zn
