View source for 2wfm


==Crystal structure of polyneuridine aldehyde esterase mutant (H244A)==
<StructureSection load='2wfm' size='340' side='right'caption='[[2wfm]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wfm]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Rauvolfia_serpentina Rauvolfia serpentina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WFM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=2wfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfm OCA], [https://pdbe.org/2wfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wfm RCSB], [https://www.ebi.ac.uk/pdbsum/2wfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wfm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PNAE_RAUSE PNAE_RAUSE] Catalyzes the hydrolysis of polyneuridine aldehyde into epi-vellosimine, which is the immediate precursor for the synthesis of the ajmaline.<ref>PMID:10691977</ref> 
== 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/wf/2wfm_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=2wfm ConSurf].
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cutting carbons: The three-dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C(9)- from C(10)-monoterpenoid indole alkaloids (see scheme). PNAE is a very substrate-specific serine esterase. It harbors the catalytic triad S87-D216-H244, and is a new member of the alpha/beta-fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures.

Structural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids.,Yang L, Hill M, Wang M, Panjikar S, Stockigt J Angew Chem Int Ed Engl. 2009;48(28):5211-3. PMID:19496101<ref>PMID:19496101</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2wfm" style="background-color:#fffaf0;"></div>

==See Also==
*[[Polyneuridine Aldehyde Esterase|Polyneuridine Aldehyde Esterase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rauvolfia serpentina]]
[[Category: Hill M]]
[[Category: Panjikar S]]
[[Category: Stoeckigt J]]
[[Category: Wang M]]
[[Category: Yang L]]