2ag8
From Proteopedia
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| - | [[Image:2ag8.gif|left|200px]] | + | [[Image:2ag8.gif|left|200px]] |
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| - | '''NADP complex of Pyrroline-5-carboxylate reductase from Neisseria meningitidis''' | + | {{Structure |
| + | |PDB= 2ag8 |SIZE=350|CAPTION= <scene name='initialview01'>2ag8</scene>, resolution 2.10Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAP:NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NAP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NADP complex of Pyrroline-5-carboxylate reductase from Neisseria meningitidis''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2AG8 is a [ | + | 2AG8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AG8 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16233902 16233902] |
[[Category: Neisseria meningitidis]] | [[Category: Neisseria meningitidis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: NAP]] | [[Category: NAP]] | ||
[[Category: mcsg]] | [[Category: mcsg]] | ||
| - | [[Category: midwest center for structural | + | [[Category: midwest center for structural genomic]] |
[[Category: protein structure initiative]] | [[Category: protein structure initiative]] | ||
[[Category: psi]] | [[Category: psi]] | ||
| - | [[Category: pyrroline-5-carboxylate reductase ]] | + | [[Category: pyrroline-5-carboxylate reductase]] |
| - | [[Category: structural | + | [[Category: structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:49:18 2008'' |
Revision as of 13:49, 20 March 2008
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| , resolution 2.10Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
NADP complex of Pyrroline-5-carboxylate reductase from Neisseria meningitidis
Overview
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.
About this Structure
2AG8 is a Single protein structure of sequence from Neisseria meningitidis. Full crystallographic information is available from OCA.
Reference
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
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