2qua: Difference between revisions

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[[Image:2qua.jpg|left|200px]]


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==Crystal structure of LipA from Serratia marcescens==
The line below this paragraph, containing "STRUCTURE_2qua", creates the "Structure Box" on the page.
<StructureSection load='2qua' size='340' side='right'caption='[[2qua]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2qua]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QUA FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<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>
{{STRUCTURE_2qua|  PDB=2qua |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qua OCA], [https://pdbe.org/2qua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qua RCSB], [https://www.ebi.ac.uk/pdbsum/2qua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qua ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q59933_SERMA Q59933_SERMA]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qu/2qua_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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=2qua ConSurf].
<div style="clear:both"></div>


'''Crystal structure of LipA from Serratia marcescens'''
==See Also==
 
*[[Lipase 3D Structures|Lipase 3D Structures]]
 
__TOC__
==Overview==
</StructureSection>
Lipase LipA from Serratia marcescens is a 613-amino acid enzyme belonging to family I.3 of lipolytic enzymes that has an important biotechnological application in the production of a chiral precursor for the coronary vasodilator diltiazem. Like other family I.3 lipases, LipA is secreted by Gram-negative bacteria via a type I secretion system and possesses 13 copies of a calcium binding tandem repeat motif, GGXGXDXUX (U, hydrophobic amino acids), in the C-terminal part of the polypeptide chain. The 1.8-A crystal structure of LipA reveals a close relation to eukaryotic lipases, whereas family I.1 and I.2 enzymes appear to be more distantly related. Interestingly, the structure shows for the N-terminal lipase domain a variation on the canonical alpha/beta hydrolase fold in an open conformation, where the putative lid helix is anchored by a Ca(2+) ion essential for activity. Another novel feature observed in this lipase structure is the presence of a helical hairpin additional to the putative lid helix that exposes a hydrophobic surface to the aqueous medium and might function as an additional lid. The tandem repeats form two separated parallel beta-roll domains that pack tightly against each other. Variations of the consensus sequence of the tandem repeats within the second beta-roll result in an asymmetric Ca(2+) binding on only one side of the roll. The analysis of the properties of the beta-roll domains suggests an intramolecular chaperone function.
[[Category: Large Structures]]
 
==About this Structure==
2QUA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QUA OCA].
 
==Reference==
A calcium-gated lid and a large beta-roll sandwich are revealed by the crystal structure of extracellular lipase from Serratia marcescens., Meier R, Drepper T, Svensson V, Jaeger KE, Baumann U, J Biol Chem. 2007 Oct 26;282(43):31477-83. Epub 2007 Aug 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17728256 17728256]
[[Category: Serratia marcescens]]
[[Category: Serratia marcescens]]
[[Category: Single protein]]
[[Category: Baumann U]]
[[Category: Triacylglycerol lipase]]
[[Category: Meier R]]
[[Category: Baumann, U.]]
[[Category: Meier, R.]]
[[Category: Alpha/beta hydrolase]]
[[Category: Beta roll]]
[[Category: Helical hairpin]]
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Retrieved from "https://proteopedia.org/2qua"