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New page: left|200px<br /><applet load="1wtj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wtj, resolution 1.55Å" /> '''Crystal Structure of...
 
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[[Image:1wtj.gif|left|200px]]<br /><applet load="1wtj" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1wtj, resolution 1.55&Aring;" />
'''Crystal Structure of delta1-piperideine-2-carboxylate reductase from Pseudomonas syringae pvar.tomato'''<br />


==Overview==
==Crystal Structure of delta1-piperideine-2-carboxylate reductase from Pseudomonas syringae pvar.tomato==
Delta(1)-Piperideine-2-carboxylate/Delta(1)-pyrroline-2-carboxylate, reductase from Pseudomonas syringae pv. tomato belongs to a novel, sub-class in a large family of NAD(P)H-dependent oxidoreductases distinct, from the conventional MDH/LDH superfamily characterized by the Rossmann, fold. We have determined the structures of the following three forms of, the enzyme: the unliganded form, the complex with NADPH, and the complex, with NADPH and pyrrole-2-carboxylate at 1.55-, 1.8-, and 1.7-A, resolutions, respectively. The enzyme exists as a dimer, and the subunit, consists of three domains; domain I, domain II (NADPH binding domain), and, domain III. The core of the NADPH binding domain consists of a, seven-stranded predominantly antiparallel beta-sheet fold (which we named, SESAS) that is characteristic of the new oxidoreductase family. The enzyme, preference for NADPH over NADH is explained by the cofactor binding site, architecture. A comparison of the overall structures revealed that the, mobile domains I and III change their conformations to produce the, catalytic form. This conformational change plays important roles in, substrate recognition and the catalytic process. The active site structure, of the catalytic form made it possible to identify the catalytic, Asp:Ser:His triad and investigate the catalytic mechanism from a, stereochemical point of view.
<StructureSection load='1wtj' size='340' side='right'caption='[[1wtj]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1wtj]] 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=1WTJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WTJ FirstGlance]. <br>
1WTJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._tomato Pseudomonas syringae pv. tomato]. Active as [http://en.wikipedia.org/wiki/Ureidoglycolate_dehydrogenase Ureidoglycolate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.154 1.1.1.154] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WTJ OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#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=1wtj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wtj OCA], [https://pdbe.org/1wtj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wtj RCSB], [https://www.ebi.ac.uk/pdbsum/1wtj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wtj ProSAT]</span></td></tr>
==Reference==
</table>
Crystal structures of Delta1-piperideine-2-carboxylate/Delta1-pyrroline-2-carboxylate reductase belonging to a new family of NAD(P)H-dependent oxidoreductases: conformational change, substrate recognition, and stereochemistry of the reaction., Goto M, Muramatsu H, Mihara H, Kurihara T, Esaki N, Omi R, Miyahara I, Hirotsu K, J Biol Chem. 2005 Dec 9;280(49):40875-84. Epub 2005 Sep 28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16192274 16192274]
== 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/wt/1wtj_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=1wtj ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas syringae pv. tomato]]
[[Category: Pseudomonas syringae pv. tomato]]
[[Category: Single protein]]
[[Category: Esaki N]]
[[Category: Ureidoglycolate dehydrogenase]]
[[Category: Goto M]]
[[Category: Esaki, N.]]
[[Category: Hirotsu K]]
[[Category: Goto, M.]]
[[Category: Kurihara T]]
[[Category: Hirotsu, K.]]
[[Category: Mihara H]]
[[Category: Kurihara, T.]]
[[Category: Miyahara I]]
[[Category: Mihara, H.]]
[[Category: Muramatsu H]]
[[Category: Miyahara, I.]]
[[Category: Omi R]]
[[Category: Muramatsu, H.]]
[[Category: Omi, R.]]
[[Category: nadph dependent enzyme]]
 
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Retrieved from "https://proteopedia.org/1wtj"