2nqt

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[[Image:2nqt.gif|left|200px]]
[[Image:2nqt.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2nqt |SIZE=350|CAPTION= <scene name='initialview01'>2nqt</scene>, resolution 1.58&Aring;
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The line below this paragraph, containing "STRUCTURE_2nqt", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CSW:CYSTEINE-S-DIOXIDE'>CSW</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetyl-gamma-glutamyl-phosphate_reductase N-acetyl-gamma-glutamyl-phosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.38 1.2.1.38] </span>
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|GENE= argC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK00436 argC], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam02774 Semialdhyde_dhC], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam01118 Semialdhyde_dh]</span>
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{{STRUCTURE_2nqt| PDB=2nqt | SCENE= }}
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|RELATEDENTRY=[[2i3a|2I3A]], [[2i3g|2I3G]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nqt OCA], [http://www.ebi.ac.uk/pdbsum/2nqt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nqt RCSB]</span>
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}}
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'''Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis at 1.58 A resolution'''
'''Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis at 1.58 A resolution'''
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[[Category: Moraidin, F.]]
[[Category: Moraidin, F.]]
[[Category: TBSGC, TB Structural Genomics Consortium.]]
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[[Category: Apoprotein]]
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[[Category: Dimer]]
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[[Category: protein structure initiative]]
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[[Category: Protein structure initiative]]
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[[Category: Psi]]
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[[Category: rossmann fold]]
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[[Category: Rossmann fold]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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[[Category: tb structural genomics consortium]]
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[[Category: Tb structural genomics consortium]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:47:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:07:00 2008''
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Revision as of 06:47, 4 May 2008

Image:2nqt.gif

Template:STRUCTURE 2nqt

Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis at 1.58 A resolution


Overview

The enzyme N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) catalyzes the nicotinamide adenine dinucleotide phosphate (NADPH)-dependent reductive dephosphorylation of N-acetyl-gamma-glutamyl-phosphate to N-acetylglutamate-gamma-semialdehyde. This reaction is part of the arginine biosynthetic pathway that is essential for some microorganisms and plants, in particular, for Mycobacterium tuberculosis (Mtb). The structures of apo MtbAGPR in the space groups P2(1)2(1)2(1) and C2 and the structure of MtbAGPR bound to the cofactor NADP(+) have been solved and analyzed. Each MtbAGPR subunit consists of alpha/beta and alpha+beta domains; NADP(+) is bound in the cleft between them. The hydrogen bonds and hydrophobic contacts between the enzyme and cofactor have been examined. Comparison of the apo and the bound enzyme structures has revealed a conformational change in MtbAGPR upon NADP(+) binding. Namely, a loop (Leu88 to His92) moves more than 5 A to confine sterically the cofactor's adenine moiety in a hydrophobic pocket. To identify the catalytically important residues in MtbAGPR, a docking of the substrate to the enzyme has been performed using the present structure of the MtbAGPR/NADP(+) complex. It reveals that residues His217 and His219 could form hydrogen bonds with the docked substrate. In addition, an ion pair could form between the substrate phosphate group and the guanidinium group of Arg114. These interactions optimally place and orient the substrate for subsequent nucleophilic attack by Cys158 on the substrate gamma-carboxyl group. His219 is the most probable general base to accept a proton from Cys158 and an adjacent ion pair interaction with the side-chain carboxyl group of Glu222 could help to stabilize the resulting positive charge on His219. For this catalytic triad to function efficiently it requires a small conformational change of the order of 1 A in the loop containing His217 and His219; this could easily result from the substrate binding.

About this Structure

2NQT is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase from Mycobacterium tuberculosis in complex with NADP(+)., Cherney LT, Cherney MM, Garen CR, Niu C, Moradian F, James MN, J Mol Biol. 2007 Apr 13;367(5):1357-69. Epub 2007 Jan 20. PMID:17316682 Page seeded by OCA on Sun May 4 09:47:44 2008

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