2ag8

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(New page: 200px<br /><applet load="2ag8" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ag8, resolution 2.10&Aring;" /> '''NADP complex of Pyrr...)
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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Joachimiak, A.]]
[[Category: Joachimiak, A.]]
[[Category: Li, H.]]
[[Category: Li, H.]]
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[[Category: MCSG, Midwest.Center.for.Structural.Genomics.]]
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[[Category: MCSG, Midwest Center for Structural Genomics.]]
[[Category: NAP]]
[[Category: NAP]]
[[Category: mcsg]]
[[Category: mcsg]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:01:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:27:08 2008''

Revision as of 14:27, 21 February 2008

Image:2ag8.gif

2ag8, resolution 2.10Å

Drag the structure with the mouse to rotate

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 with as ligand. 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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