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1hl7

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Revision as of 14:29, 15 November 2017

Gamma lactamase from an Aureobacterium species in complex with 3a,4,7,7a-tetrahydro-benzo [1,3] dioxol-2-one

Structural highlights

1hl7 is a 2 chain structure with sequence from Aureobacterium sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1hkh
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The structure of the recombinant (-) gamma-lactamase from an Aureobacterium species has been solved at 1.73A resolution in the cubic space group F23 with unit cell parameters a=b=c=240.6A. The trimeric enzyme has an alpha/beta hydrolase fold and closely resembles the cofactor free haloperoxidases. The structure has been solved in complex with a covalently bound ligand originating from the host cell and also in the unligated form. The associated density in the former structure has been interpreted as the two-ring ligand (3aR,7aS)-3a,4,7,7a-tetrahydro-benzo [1,3] dioxol-2-one which forms a tetrahedral complex with OG of the catalytic Ser98. Soaks of these crystals with the industrial substrate gamma-lactam or its structural analogue, norcamphor, result in the displacement of the ligand from the enzyme active site, thereby allowing determination of the unligated structure. The presence of the ligand in the active site protects the enzyme from serine hydrolase inhibitors. Cyclic ethylene carbonate, the first ring of the ligand, was shown to be a substrate of the enzyme.

The crystal structure of a (-) gamma-lactamase from an Aureobacterium species reveals a tetrahedral intermediate in the active site.,Line K, Isupov MN, Littlechild JA J Mol Biol. 2004 Apr 30;338(3):519-32. PMID:15081810^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Line K, Isupov MN, Littlechild JA. The crystal structure of a (-) gamma-lactamase from an Aureobacterium species reveals a tetrahedral intermediate in the active site. J Mol Biol. 2004 Apr 30;338(3):519-32. PMID:15081810 doi:10.1016/j.jmb.2004.03.001

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hl7"

@@ Line 1: / Line 1: @@
 ==Gamma lactamase from an Aureobacterium species in complex with 3a,4,7,7a-tetrahydro-benzo [1,3] dioxol-2-one==
 <StructureSection load='1hl7' size='340' side='right' caption='[[1hl7]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BD1:3A,4,7,7A-TETRAHYDRO-BENZO+[1,3]+DIOXOL-2-ONE'>BD1</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hkh|1hkh]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hl7 OCA], [http://pdbe.org/1hl7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hl7 RCSB], [http://www.ebi.ac.uk/pdbsum/1hl7 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hl7 OCA], [http://pdbe.org/1hl7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hl7 RCSB], [http://www.ebi.ac.uk/pdbsum/1hl7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hl7 ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==

1hl7

From Proteopedia

Revision as of 14:29, 15 November 2017

Gamma lactamase from an Aureobacterium species in complex with 3a,4,7,7a-tetrahydro-benzo [1,3] dioxol-2-one

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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