2ag8

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[[Image:2ag8.gif|left|200px]]
 
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==NADP complex of Pyrroline-5-carboxylate reductase from Neisseria meningitidis==
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The line below this paragraph, containing "STRUCTURE_2ag8", creates the "Structure Box" on the page.
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<StructureSection load='2ag8' size='340' side='right'caption='[[2ag8]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2ag8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_MC58 Neisseria meningitidis MC58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AG8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AG8 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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{{STRUCTURE_2ag8| PDB=2ag8 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ag8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ag8 OCA], [https://pdbe.org/2ag8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ag8 RCSB], [https://www.ebi.ac.uk/pdbsum/2ag8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ag8 ProSAT], [https://www.topsan.org/Proteins/MCSG/2ag8 TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9K1N1_NEIMB Q9K1N1_NEIMB]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ag/2ag8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ag8 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''NADP complex of Pyrroline-5-carboxylate reductase from Neisseria meningitidis'''
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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<ref>PMID:16233902</ref>
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==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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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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].
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</div>
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<div class="pdbe-citations 2ag8" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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]
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*[[Pyrroline-5-carboxylate reductase|Pyrroline-5-carboxylate reductase]]
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[[Category: Neisseria meningitidis]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Chang, C.]]
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__TOC__
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[[Category: Collart, F.]]
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</StructureSection>
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[[Category: Joachimiak, A.]]
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[[Category: Large Structures]]
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[[Category: Li, H.]]
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[[Category: Neisseria meningitidis MC58]]
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[[Category: MCSG, Midwest Center for Structural Genomics.]]
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[[Category: Chang C]]
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[[Category: Mcsg]]
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[[Category: Collart F]]
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[[Category: Midwest center for structural genomic]]
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[[Category: Joachimiak A]]
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[[Category: Protein structure initiative]]
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[[Category: Li H]]
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[[Category: Psi]]
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[[Category: Pyrroline-5-carboxylate reductase]]
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[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:00:42 2008''
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Current revision

NADP complex of Pyrroline-5-carboxylate reductase from Neisseria meningitidis

PDB ID 2ag8

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