3ia2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "3ia2" [edit=sysop:move=sysop])
Line 1: Line 1:
-
[[Image:3ia2.png|left|200px]]
+
==Pseudomonas fluorescens esterase complexed to the R-enantiomer of a sulfonate transition state analog==
 +
<StructureSection load='3ia2' size='340' side='right' caption='[[3ia2]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3ia2]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IA2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IA2 FirstGlance]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=J6Z:(2R)-BUTANE-2-SULFONATE'>J6Z</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
 +
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1va4|1va4]], [[3hea|3hea]]</td></tr>
 +
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ia2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ia2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ia2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ia2 PDBsum]</span></td></tr>
 +
<table>
 +
== 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/ia/3ia2_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/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Acyl transfer is a key reaction in biosynthesis, including synthesis of antibiotics and polyesters. Although researchers have long recognized the similar protein fold and catalytic machinery in acyltransferases and hydrolases, the molecular basis for the different reactivity has been a long-standing mystery. By comparison of X-ray structures, we identified a different oxyanion-loop orientation in the active site. In esterases/lipases a carbonyl oxygen points toward the active site, whereas in acyltransferases a NH of the main-chain amide points toward the active site. Amino acid sequence comparisons alone cannot identify such a difference in the main-chain orientation. To identify how this difference might change the reaction mechanism, we solved the X-ray crystal structure of Pseudomonas fluorescens esterase containing a sulfonate transition-state analogue bound to the active-site serine. This structure mimics the transition state for the attack of water on the acyl-enzyme and shows a bridging water molecule between the carbonyl oxygen mentioned above and the sulfonyl oxygen that mimics the attacking water. A possible mechanistic role for this bridging water molecule is to position and activate the attacking water molecule in hydrolases, but to deactivate the attacking water molecule in acyl transferases.
-
<!--
+
Different active-site loop orientation in serine hydrolases versus acyltransferases.,Jiang Y, Morley KL, Schrag JD, Kazlauskas RJ Chembiochem. 2011 Mar 21;12(5):768-76. doi: 10.1002/cbic.201000693. Epub, 2011 Feb 23. PMID:21351219<ref>PMID:21351219</ref>
-
The line below this paragraph, containing "STRUCTURE_3ia2", creates the "Structure Box" on the page.
+
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
-
or leave the SCENE parameter empty for the default display.
+
-
-->
+
-
{{STRUCTURE_3ia2| PDB=3ia2 | SCENE= }}
+
-
===Pseudomonas fluorescens esterase complexed to the R-enantiomer of a sulfonate transition state analog===
+
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
 
+
== References ==
-
<!--
+
<references/>
-
The line below this paragraph, {{ABSTRACT_PUBMED_21351219}}, adds the Publication Abstract to the page
+
__TOC__
-
(as it appears on PubMed at http://www.pubmed.gov), where 21351219 is the PubMed ID number.
+
</StructureSection>
-
-->
+
-
{{ABSTRACT_PUBMED_21351219}}
+
-
 
+
-
==About this Structure==
+
-
[[3ia2]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IA2 OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:021351219</ref><references group="xtra"/>
+
[[Category: Pseudomonas fluorescens]]
[[Category: Pseudomonas fluorescens]]
[[Category: Jiang, Y.]]
[[Category: Jiang, Y.]]

Revision as of 09:47, 21 May 2014

Pseudomonas fluorescens esterase complexed to the R-enantiomer of a sulfonate transition state analog

3ia2, resolution 1.65Å

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/3ia2"
Views
Personal tools
Navigation
Toolbox