View source for 2cwf


==Crystal Structure of delta1-piperideine-2-carboxylate reductase from Pseudomonas syringae complexed with NADPH==
<StructureSection load='2cwf' size='340' side='right'caption='[[2cwf]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2cwf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._tomato Pseudomonas syringae pv. tomato]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CWF 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></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=2cwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cwf OCA], [https://pdbe.org/2cwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cwf RCSB], [https://www.ebi.ac.uk/pdbsum/2cwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cwf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PY2CR_PSEUB PY2CR_PSEUB] Catalyzes the reduction of both Delta(1)-pyrroline-2-carboxylate (Pyr2C) and Delta(1)-piperideine-2-carboxylate (Pip2C) to L-proline and L-pipecolate, respectively, using NADPH as the electron donor. Can catalyze the reverse oxidation reactions, albeit at a much lower rate. Is also able to catalyze in vitro the NADPH-dependent formation of N-methylalanine from pyruvate and N-methylamine; can act on other alpha-keto acids and specifically uses methylamine and not ammonia for these reductive amination reactions. Can use NADH instead of NADPH, although with much less efficiency.<ref>PMID:16192274</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/cw/2cwf_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=2cwf ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas syringae pv. tomato]]
[[Category: Esaki N]]
[[Category: Goto M]]
[[Category: Hirotsu K]]
[[Category: Kurihara T]]
[[Category: Mihara H]]
[[Category: Miyahara I]]
[[Category: Muramatsu H]]
[[Category: Omi R]]