1qge: Difference between revisions

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<StructureSection load='1qge' size='340' side='right'caption='[[1qge]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1qge' size='340' side='right'caption='[[1qge]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1qge]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_glumae Burkholderia glumae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QGE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QGE FirstGlance]. <br>
<table><tr><td colspan='2'>[[1qge]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_glumae Burkholderia glumae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QGE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QGE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=1qge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qge OCA], [http://pdbe.org/1qge PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qge RCSB], [http://www.ebi.ac.uk/pdbsum/1qge PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qge ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qge OCA], [https://pdbe.org/1qge PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qge RCSB], [https://www.ebi.ac.uk/pdbsum/1qge PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qge ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/LIP_BURGL LIP_BURGL]] Catalyzes the hydrolysis of triglycerides.  
[https://www.uniprot.org/uniprot/LIP_PSEPS LIP_PSEPS] Catalyzes the hydrolysis of triacylglycerol.<ref>PMID:7786905</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qg/1qge_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qg/1qge_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qge ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qge ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of a lipase from the bacterium Chromobacterium viscosum ATCC 6918 (CVL) has been determined by isomorphous replacement and refined at 1.6 angstroms resolution to an R-factor of 17.8%. The lipase has the overall topology of an alpha/beta type protein, which was also found for previously determined lipase structures. The catalytic triad of the active center consists of the residues Ser87, Asp263 and His285. These residues are not exposed to the solvent, but a narrow channel connects them with the molecular surface. This conformation is very similar to the previously reported closed conformation of Pseudomonas glumae lipase (PGL), but superposition of the two lipase structures reveals several conformational differences. r.m.s. deviations greater than 2 angstroms are found for the C alpha-atoms of the polypeptide chains from His15 to Asp28, from Leu49 to Ser54 and from Lys128 to Gln158. Compared to the PGL structure in the CVL structure, three alpha-helical fragments are shorter, one beta-strand is longer and an additional antiparallel beta-sheet is found. In contrast to PGL, CVL displays an oxyanion hole, which is stabilized by the amide nitrogen atoms of Leu17 and Gln88, and a cis-peptide bond between Gln291 and Leu292. CVL contains a Ca2+, like the PGL, which is coordinated by four oxygen atoms from the protein and two water molecules.
Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6 angstroms resolution.,Lang D, Hofmann B, Haalck L, Hecht HJ, Spener F, Schmid RD, Schomburg D J Mol Biol. 1996 Jun 21;259(4):704-17. PMID:8683577<ref>PMID:8683577</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1qge" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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[[Category: Burkholderia glumae]]
[[Category: Burkholderia glumae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Triacylglycerol lipase]]
[[Category: Dijkstra BW]]
[[Category: Dijkstra, B W]]
[[Category: Kovacs A]]
[[Category: Kovacs, A]]
[[Category: Lang DA]]
[[Category: Lang, D A]]
[[Category: Paltauf F]]
[[Category: Paltauf, F]]
[[Category: Stadler P]]
[[Category: Stadler, P]]
[[Category: Cis-peptide]]
[[Category: Closed conformation]]
[[Category: Hydrolase]]
[[Category: Lid]]
[[Category: Pseudomonadaceae]]

Latest revision as of 10:15, 30 October 2024

NEW CRYSTAL FORM OF PSEUDOMONAS GLUMAE (FORMERLY CHROMOBACTERIUM VISCOSUM ATCC 6918) LIPASENEW CRYSTAL FORM OF PSEUDOMONAS GLUMAE (FORMERLY CHROMOBACTERIUM VISCOSUM ATCC 6918) LIPASE

Structural highlights

1qge is a 2 chain structure with sequence from Burkholderia glumae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LIP_PSEPS Catalyzes the hydrolysis of triacylglycerol.[1]

Evolutionary Conservation

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

See Also

References

  1. ↑ Taipa MA, Liebeton K, Costa JV, Cabral JM, Jaeger KE. Lipase from Chromobacterium viscosum: biochemical characterization indicating homology to the lipase from Pseudomonas glumae. Biochim Biophys Acta. 1995 Jun 6;1256(3):396-402. PMID:7786905 doi:10.1016/0005-2760(95)00052-e

1qge, resolution 1.70Å

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