2cwf: Difference between revisions

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<StructureSection load='2cwf' size='340' side='right'caption='[[2cwf]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='2cwf' size='340' side='right'caption='[[2cwf]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2cwf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cfbp_2212 Cfbp 2212]. 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>
<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='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>
</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2cwh|2cwh]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dpkA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=323 CFBP 2212])</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>
<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>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/Q4U331_PSEUB Q4U331_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>
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:16192274<ref>PMID:16192274</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2cwf" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cfbp 2212]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Esaki, N]]
[[Category: Pseudomonas syringae pv. tomato]]
[[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: Nadph dependent enzyme]]
[[Category: Omi R]]
[[Category: Oxidoreductase]]
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