2ahr: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ahr]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AHR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AHR FirstGlance]. <br> | <table><tr><td colspan='2'>[[2ahr]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AHR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AHR FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yqg|1yqg]], [[2ag8|2ag8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yqg|1yqg]], [[2ag8|2ag8]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ahr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ahr RCSB], [http://www.ebi.ac.uk/pdbsum/2ahr PDBsum], [http://www.topsan.org/Proteins/MCSG/2ahr TOPSAN]</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=2ahr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ahr RCSB], [http://www.ebi.ac.uk/pdbsum/2ahr PDBsum], [http://www.topsan.org/Proteins/MCSG/2ahr TOPSAN]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Pyrroline-5-carboxylate reductase]] | [[Category: Pyrroline-5-carboxylate reductase]] | ||
[[Category: Streptococcus pyogenes]] | [[Category: Streptococcus pyogenes]] | ||
[[Category: Holzle, D | [[Category: Holzle, D]] | ||
[[Category: Joachimiak, A | [[Category: Joachimiak, A]] | ||
[[Category: Lezondra, L | [[Category: Lezondra, L]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Nocek, B | [[Category: Nocek, B]] | ||
[[Category: 1-pyrroline-5-carboxylate reductase]] | [[Category: 1-pyrroline-5-carboxylate reductase]] | ||
[[Category: Doain swapping]] | [[Category: Doain swapping]] | ||
[[Category: Human pathogen]] | [[Category: Human pathogen]] | ||
[[Category: Mcsg]] | [[Category: Mcsg]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Proline biosynthesis]] | [[Category: Proline biosynthesis]] | ||
[[Category: Protein structure initiative | [[Category: PSI, Protein structure initiative]] | ||
[[Category: Pyrroline reductase]] | [[Category: Pyrroline reductase]] | ||
[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||
[[Category: Streptococcus pyogene]] | [[Category: Streptococcus pyogene]] | ||
Revision as of 12:47, 8 January 2015
Crystal Structures of 1-Pyrroline-5-Carboxylate Reductase from Human Pathogen Streptococcus pyogenesCrystal Structures of 1-Pyrroline-5-Carboxylate Reductase from Human Pathogen Streptococcus pyogenes
Structural highlights
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 PubMedL-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 AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pyrroline-5-carboxylate reductase
- Streptococcus pyogenes
- Holzle, D
- Joachimiak, A
- Lezondra, L
- Structural genomic
- Nocek, B
- 1-pyrroline-5-carboxylate reductase
- Doain swapping
- Human pathogen
- Mcsg
- Oxidoreductase
- Proline biosynthesis
- PSI, Protein structure initiative
- Pyrroline reductase
- Rossmann fold
- Streptococcus pyogene