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[[Image:2ger.gif|left|200px]]
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{{STRUCTURE_2ger|  PDB=2ger  |  SCENE=  }}
'''Crystal Structure and Oxidative Mechanism of Human Pyrroline-5-carboxylate Reductase'''


==Crystal Structure and Oxidative Mechanism of Human Pyrroline-5-carboxylate Reductase==
<StructureSection load='2ger' size='340' side='right'caption='[[2ger]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ger]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GER 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]] 3.1&#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=2ger FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ger OCA], [https://pdbe.org/2ger PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ger RCSB], [https://www.ebi.ac.uk/pdbsum/2ger PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ger ProSAT]</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/ge/2ger_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2ger ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pyrroline-5-carboxylate reductase (P5CR) is a universal housekeeping enzyme that catalyzes the reduction of Delta(1)-pyrroline-5-carboxylate (P5C) to proline using NAD(P)H as the cofactor. The enzymatic cycle between P5C and proline is very important for the regulation of amino acid metabolism, intracellular redox potential, and apoptosis. Here, we present the 2.8 Angstroms resolution structure of the P5CR apo enzyme, its 3.1 Angstroms resolution ternary complex with NAD(P)H and substrate-analog. The refined structures demonstrate a decameric architecture with five homodimer subunits and ten catalytic sites arranged around a peripheral circular groove. Mutagenesis and kinetic studies reveal the pivotal roles of the dinucleotide-binding Rossmann motif and residue Glu221 in the human enzyme. Human P5CR is thermostable and the crystals were grown at 37 degrees C. The enzyme is implicated in oxidation of the anti-tumor drug thioproline.


==Overview==
Crystal structure of human pyrroline-5-carboxylate reductase.,Meng Z, Lou Z, Liu Z, Li M, Zhao X, Bartlam M, Rao Z J Mol Biol. 2006 Jun 23;359(5):1364-77. Epub 2006 May 11. PMID:16730026<ref>PMID:16730026</ref>
Pyrroline-5-carboxylate reductase (P5CR) is a universal housekeeping enzyme that catalyzes the reduction of Delta(1)-pyrroline-5-carboxylate (P5C) to proline using NAD(P)H as the cofactor. The enzymatic cycle between P5C and proline is very important for the regulation of amino acid metabolism, intracellular redox potential, and apoptosis. Here, we present the 2.8 Angstroms resolution structure of the P5CR apo enzyme, its 3.1 Angstroms resolution ternary complex with NAD(P)H and substrate-analog. The refined structures demonstrate a decameric architecture with five homodimer subunits and ten catalytic sites arranged around a peripheral circular groove. Mutagenesis and kinetic studies reveal the pivotal roles of the dinucleotide-binding Rossmann motif and residue Glu221 in the human enzyme. Human P5CR is thermostable and the crystals were grown at 37 degrees C. The enzyme is implicated in oxidation of the anti-tumor drug thioproline.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2GER is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GER OCA].
</div>
<div class="pdbe-citations 2ger" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structure of human pyrroline-5-carboxylate reductase., Meng Z, Lou Z, Liu Z, Li M, Zhao X, Bartlam M, Rao Z, J Mol Biol. 2006 Jun 23;359(5):1364-77. Epub 2006 May 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16730026 16730026]
*[[Pyrroline-5-carboxylate reductase|Pyrroline-5-carboxylate reductase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Pyrroline-5-carboxylate reductase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Liu Z]]
[[Category: Liu, Z.]]
[[Category: Lou Z]]
[[Category: Lou, Z.]]
[[Category: Meng Z]]
[[Category: Meng, Z.]]
[[Category: Rao Z]]
[[Category: Rao, Z.]]
[[Category: Crystal structure,oxidative mechanism of human pyrroline-5-carboxylate]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:01:11 2008''

Latest revision as of 00:58, 21 November 2024

Crystal Structure and Oxidative Mechanism of Human Pyrroline-5-carboxylate Reductase

2ger, resolution 3.10Å

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