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| | ==Crystal structure of 1-Pyrroline-5-Carboxylate Reductase from Human Pathogen Streptococcus Pyogenes== | | ==Crystal structure of 1-Pyrroline-5-Carboxylate Reductase from Human Pathogen Streptococcus Pyogenes== |
| - | <StructureSection load='2amf' size='340' side='right' caption='[[2amf]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='2amf' size='340' side='right'caption='[[2amf]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2amf]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes_(serotype_1_/_m1_gas) Streptococcus pyogenes (serotype 1 / m1 gas)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AMF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AMF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2amf]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes_M1_GAS Streptococcus pyogenes M1 GAS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AMF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</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]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yqg|1yqg]], [[2ag8|2ag8]], [[2ahr|2ahr]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">proC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=160490 Streptococcus pyogenes (serotype 1 / M1 GAS)])</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=2amf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2amf OCA], [https://pdbe.org/2amf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2amf RCSB], [https://www.ebi.ac.uk/pdbsum/2amf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2amf ProSAT], [https://www.topsan.org/Proteins/MCSG/2amf TOPSAN]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_(NAD(P)(+)) Aldehyde dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.5 1.2.1.5] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2amf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2amf OCA], [http://pdbe.org/2amf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2amf RCSB], [http://www.ebi.ac.uk/pdbsum/2amf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2amf ProSAT], [http://www.topsan.org/Proteins/MCSG/2amf TOPSAN]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9A1S9_STRP1 Q9A1S9_STRP1] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/am/2amf_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/am/2amf_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Holzle, D]] | + | [[Category: Large Structures]] |
| - | [[Category: Joachimiak, A]] | + | [[Category: Streptococcus pyogenes M1 GAS]] |
| - | [[Category: Lezondra, L]] | + | [[Category: Holzle D]] |
| - | [[Category: Structural genomic]] | + | [[Category: Joachimiak A]] |
| - | [[Category: Nocek, B]] | + | [[Category: Lezondra L]] |
| - | [[Category: 1-pyrroline-5-reductase]] | + | [[Category: Nocek B]] |
| - | [[Category: Domain swapping]]
| + | |
| - | [[Category: Human pathogen]]
| + | |
| - | [[Category: Mcsg]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Proline biosynthesis]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Pyrroline reductase]]
| + | |
| - | [[Category: Pyrroline-5-carboxylate reductase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| - | [[Category: Streptococcus pyogene]]
| + | |
| Structural highlights
Function
Q9A1S9_STRP1
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
L-proline is an amino acid that plays an important role in proteins uniquely contributing to protein folding, structure, and stability, and this amino acid serves as a sequence-recognition motif. Proline biosynthesis can occur via two pathways, one from glutamate and the other from arginine. In both pathways, the last step of biosynthesis, the conversion of delta1-pyrroline-5-carboxylate (P5C) to L-proline, is catalyzed by delta1-pyrroline-5-carboxylate reductase (P5CR) using NAD(P)H as a cofactor. We have determined the first crystal structure of P5CR from two human pathogens, Neisseria meningitides and Streptococcus pyogenes, at 2.0 angstroms and 2.15 angstroms resolution, respectively. The catalytic unit of P5CR is a dimer composed of two domains, but the biological unit seems to be species-specific. The N-terminal domain of P5CR is an alpha/beta/alpha sandwich, a Rossmann fold. The C-terminal dimerization domain is rich in alpha-helices and shows domain swapping. Comparison of the native structure of P5CR to structures complexed with L-proline and NADP+ in two quite different primary sequence backgrounds provides unique information about key functional features: the active site and the catalytic mechanism. The inhibitory L-proline has been observed in the crystal structure.
Crystal structures of delta1-pyrroline-5-carboxylate reductase from human pathogens Neisseria meningitides and Streptococcus pyogenes.,Nocek B, Chang C, Li H, Lezondra L, Holzle D, Collart F, Joachimiak A J Mol Biol. 2005 Nov 18;354(1):91-106. Epub 2005 Sep 2. PMID:16233902[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nocek B, Chang C, Li H, Lezondra L, Holzle D, Collart F, Joachimiak A. Crystal structures of delta1-pyrroline-5-carboxylate reductase from human pathogens Neisseria meningitides and Streptococcus pyogenes. J Mol Biol. 2005 Nov 18;354(1):91-106. Epub 2005 Sep 2. PMID:16233902 doi:10.1016/j.jmb.2005.08.036
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