1k07: Difference between revisions
New page: left|200px<br /><applet load="1k07" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k07, resolution 1.65Å" /> '''Native FEZ-1 metallo... |
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[[Image:1k07.gif|left|200px]]<br /><applet load="1k07" size=" | [[Image:1k07.gif|left|200px]]<br /><applet load="1k07" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1k07, resolution 1.65Å" /> | caption="1k07, resolution 1.65Å" /> | ||
'''Native FEZ-1 metallo-beta-lactamase from Legionella gormanii'''<br /> | '''Native FEZ-1 metallo-beta-lactamase from Legionella gormanii'''<br /> | ||
==Overview== | ==Overview== | ||
The beta-lactamases are involved in bacterial resistance to penicillin and | The beta-lactamases are involved in bacterial resistance to penicillin and related compounds. Members of the metallo-enzyme class are now found in many pathogenic bacteria and are thus becoming of major clinical importance. The structures of the Zn-beta-lactamase from Fluoribacter gormanii (FEZ-1) in the native and in the complex form are reported here. FEZ-1 is a monomeric enzyme, which possesses two zinc-binding sites. These structures are discussed in comparison with those of the tetrameric L1 enzyme produced by Stenotrophomonas maltophilia. From this analysis, amino acids involved in the oligomerization of L1 are clearly identified. Despite the similarity in fold, the active site of FEZ-1 was found to be significantly different. Two residues, which were previously implicated in function, are not present in L1 or in FEZ-1. The broad-spectrum substrate profile of Zn-beta-lactamases arises from the rather wide active-site cleft, where various beta-lactam compounds can be accommodated. | ||
==About this Structure== | ==About this Structure== | ||
1K07 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fluoribacter_gormanii Fluoribacter gormanii] with ZN, SO4, ACT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | 1K07 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fluoribacter_gormanii Fluoribacter gormanii] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K07 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dideberg, O.]] | [[Category: Dideberg, O.]] | ||
[[Category: Frere, J | [[Category: Frere, J M.]] | ||
[[Category: Galleni, M.]] | [[Category: Galleni, M.]] | ||
[[Category: Garcia-Saez, I.]] | [[Category: Garcia-Saez, I.]] | ||
[[Category: Kahn, R.]] | [[Category: Kahn, R.]] | ||
[[Category: Mercuri, P | [[Category: Mercuri, P S.]] | ||
[[Category: Papamicael, C.]] | [[Category: Papamicael, C.]] | ||
[[Category: ACT]] | [[Category: ACT]] | ||
| Line 27: | Line 27: | ||
[[Category: monomer with alpha-beta/beta-alpha fold. two monomers per assymmetric unit.]] | [[Category: monomer with alpha-beta/beta-alpha fold. two monomers per assymmetric unit.]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:39 2008'' | ||
Revision as of 14:28, 21 February 2008
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Native FEZ-1 metallo-beta-lactamase from Legionella gormanii
OverviewOverview
The beta-lactamases are involved in bacterial resistance to penicillin and related compounds. Members of the metallo-enzyme class are now found in many pathogenic bacteria and are thus becoming of major clinical importance. The structures of the Zn-beta-lactamase from Fluoribacter gormanii (FEZ-1) in the native and in the complex form are reported here. FEZ-1 is a monomeric enzyme, which possesses two zinc-binding sites. These structures are discussed in comparison with those of the tetrameric L1 enzyme produced by Stenotrophomonas maltophilia. From this analysis, amino acids involved in the oligomerization of L1 are clearly identified. Despite the similarity in fold, the active site of FEZ-1 was found to be significantly different. Two residues, which were previously implicated in function, are not present in L1 or in FEZ-1. The broad-spectrum substrate profile of Zn-beta-lactamases arises from the rather wide active-site cleft, where various beta-lactam compounds can be accommodated.
About this StructureAbout this Structure
1K07 is a Single protein structure of sequence from Fluoribacter gormanii with , , and as ligands. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril., Garcia-Saez I, Mercuri PS, Papamicael C, Kahn R, Frere JM, Galleni M, Rossolini GM, Dideberg O, J Mol Biol. 2003 Jan 24;325(4):651-60. PMID:12507470
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