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2ger

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(New page: 200px<br /> <applet load="2ger" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ger, resolution 3.1&Aring;" /> '''Crystal Structure an...)
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[[Image:2ger.gif|left|200px]]<br />
 
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<applet load="2ger" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ger, resolution 3.1&Aring;" />
 
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'''Crystal Structure and Oxidative Mechanism of Human Pyrroline-5-carboxylate Reductase'''<br />
 
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==Overview==
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==Crystal Structure and Oxidative Mechanism of Human Pyrroline-5-carboxylate Reductase==
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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.
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<StructureSection load='2ger' size='340' side='right'caption='[[2ger]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2ger]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pyrroline-5-carboxylate_reductase Pyrroline-5-carboxylate reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.2 1.5.1.2] </span></td></tr>
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<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>
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</table>
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== Disease ==
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[[https://www.uniprot.org/uniprot/P5CR1_HUMAN P5CR1_HUMAN]] Defects in PYCR1 are the cause of cutis laxa autosomal recessive type 2B (ARCL2B) [MIM:[https://omim.org/entry/612940 612940]]. A multisystem disorder characterized by the appearance of premature aging, wrinkled and lax skin with reduced elasticity, joint laxity, craniofacial dysmorphic features, intrauterine growth retardation with some degree of postnatal growth deficiency, and developmental delay.<ref>PMID:19648921</ref> <ref>PMID:19576563</ref> Defects in PYCR1 are the cause of cutis laxa, autosomal recessive, type 3B (ARCL3B) [MIM:[https://omim.org/entry/614438 614438]]. ARCL3B is a disorder characterized by an aged appearance with distinctive facial features, sparse hair, ophthalmologic abnormalities, intrauterine growth retardation, and cutis laxa.<ref>PMID:19648921</ref> <ref>PMID:22052856</ref>
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== Function ==
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[[https://www.uniprot.org/uniprot/P5CR1_HUMAN P5CR1_HUMAN]] Housekeeping enzyme that catalyzes the last step in proline biosynthesis. Can utilize both NAD and NADP, but has higher affinity for NAD. Involved in the cellular response to oxidative stress.<ref>PMID:19648921</ref> <ref>PMID:16730026</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ge/2ger_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2ger ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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2GER is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Pyrroline-5-carboxylate_reductase Pyrroline-5-carboxylate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.2 1.5.1.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GER OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16730026 16730026]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 2ger" style="background-color:#fffaf0;"></div>
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[[Category: Pyrroline-5-carboxylate reductase]]
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[[Category: Single protein]]
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[[Category: Liu, Z.]]
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[[Category: Lou, Z.]]
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[[Category: Meng, Z.]]
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[[Category: Rao, Z.]]
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[[Category: crystal structure]]
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[[Category: oxidative mechanism of human pyrroline-5-carboxylate]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:17:57 2007''
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==See Also==
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*[[Pyrroline-5-carboxylate reductase|Pyrroline-5-carboxylate reductase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Human]]
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[[Category: Large Structures]]
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[[Category: Pyrroline-5-carboxylate reductase]]
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[[Category: Liu, Z]]
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[[Category: Lou, Z]]
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[[Category: Meng, Z]]
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[[Category: Rao, Z]]
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[[Category: Oxidative mechanism of human pyrroline-5-carboxylate]]
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[[Category: Oxidoreductase]]

Current revision

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

PDB ID 2ger

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