2ag8
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2ag8.gif|left|200px]] | [[Image:2ag8.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2ag8", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_2ag8| PDB=2ag8 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''NADP complex of Pyrroline-5-carboxylate reductase from Neisseria meningitidis''' | '''NADP complex of Pyrroline-5-carboxylate reductase from Neisseria meningitidis''' | ||
| Line 30: | Line 27: | ||
[[Category: Li, H.]] | [[Category: Li, H.]] | ||
[[Category: MCSG, Midwest Center for Structural Genomics.]] | [[Category: MCSG, Midwest Center for Structural Genomics.]] | ||
| - | [[Category: | + | [[Category: Mcsg]] |
| - | [[Category: | + | [[Category: Midwest center for structural genomic]] |
| - | [[Category: | + | [[Category: Protein structure initiative]] |
| - | [[Category: | + | [[Category: Psi]] |
| - | [[Category: | + | [[Category: Pyrroline-5-carboxylate reductase]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:00:42 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:00, 3 May 2008
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 Page seeded by OCA on Sat May 3 19:00:42 2008
