2hih

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:51, 25 October 2023) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2hih.png|left|200px]]
 
-
<!--
+
==Crystal structure of Staphylococcus hyicus lipase==
-
The line below this paragraph, containing "STRUCTURE_2hih", creates the "Structure Box" on the page.
+
<StructureSection load='2hih' size='340' side='right'caption='[[2hih]], [[Resolution|resolution]] 2.86&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'>[[2hih]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_hyicus Staphylococcus hyicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HIH 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]] 2.86&#8491;</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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
{{STRUCTURE_2hih| PDB=2hih | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hih OCA], [https://pdbe.org/2hih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hih RCSB], [https://www.ebi.ac.uk/pdbsum/2hih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hih ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/LIP_STAHY LIP_STAHY]
 +
== 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/hi/2hih_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=2hih ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Staphylococcus hyicus lipase differs from other bacterial lipases in its high phospholipase A1 activity. Here, we present the crystal structure of the S. hyicus lipase at 2.86 A resolution. The lipase is in an open conformation, with the active site partly covered by a neighbouring molecule. Ser124, Asp314 and His355 form the catalytic triad. The substrate-binding cavity contains two large hydrophobic acyl chain-binding pockets and a shallow and more polar third pocket that is capable of binding either a (short) fatty acid or a phospholipid head-group. A model of a phospholipid bound in the active site shows that Lys295 is at hydrogen bonding distance from the substrate's phosphate group. Residues Ser356, Glu292 and Thr294 hold the lysine in position by hydrogen bonding and electrostatic interactions. These observations explain the biochemical data showing the importance of Lys295 and Ser356 for phospholipid binding and phospholipase A1 activity.
-
===Crystal structure of Staphylococcus hyicus lipase===
+
Structural basis of phospholipase activity of Staphylococcus hyicus lipase.,Tiesinga JJ, van Pouderoyen G, Nardini M, Ransac S, Dijkstra BW J Mol Biol. 2007 Aug 10;371(2):447-56. Epub 2007 May 21. PMID:17582438<ref>PMID:17582438</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2hih" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_17582438}}, adds the Publication Abstract to the page
+
*[[Lipase 3D Structures|Lipase 3D Structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 17582438 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_17582438}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
2HIH is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Staphylococcus_hyicus Staphylococcus hyicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HIH OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:17582438</ref><references group="xtra"/>
+
[[Category: Staphylococcus hyicus]]
[[Category: Staphylococcus hyicus]]
-
[[Category: Triacylglycerol lipase]]
+
[[Category: Dijkstra BW]]
-
[[Category: Dijkstra, B W.]]
+
[[Category: Nardini M]]
-
[[Category: Nardini, M.]]
+
[[Category: Tiesinga JJW]]
-
[[Category: Pouderoyen, G van.]]
+
[[Category: Van Pouderoyen G]]
-
[[Category: Tiesinga, J J.W.]]
+
-
[[Category: A1 phospholipase]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Lipase]]
+
-
[[Category: Phospholipid binding]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 11 11:22:02 2009''
+

Current revision

Crystal structure of Staphylococcus hyicus lipase

PDB ID 2hih

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hih"
Personal tools