1gsj
From Proteopedia
(Difference between revisions)
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<StructureSection load='1gsj' size='340' side='right'caption='[[1gsj]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='1gsj' size='340' side='right'caption='[[1gsj]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1gsj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1gsj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GSJ FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NLG:N-ACETYL-L-GLUTAMATE'>NLG</scene></td></tr> |
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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=1gsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gsj OCA], [https://pdbe.org/1gsj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gsj RCSB], [https://www.ebi.ac.uk/pdbsum/1gsj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gsj ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gsj OCA], [https://pdbe.org/1gsj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gsj RCSB], [https://www.ebi.ac.uk/pdbsum/1gsj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gsj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/ARGB_ECOLI ARGB_ECOLI] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1gsj ConSurf]. | </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=1gsj ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | N-Acetyl-L-glutamate kinase (NAGK), a member of the amino acid kinase family, catalyzes the second and frequently controlling step of arginine synthesis. The Escherichia coli NAGK crystal structure to 1.5 A resolution reveals a 258-residue subunit homodimer nucleated by a central 16-stranded molecular open beta sheet sandwiched between alpha helices. In each subunit, AMPPNP, as an alphabetagamma-phosphate-Mg2+ complex, binds along the sheet C edge, and N-acetyl-L-glutamate binds near the dyadic axis with its gamma-COO- aligned at short distance from the gamma-phosphoryl, indicating associative phosphoryl transfer assisted by: (1) Mg2+ complexation; (2) the positive charges on Lys8, Lys217, and on two helix dipoles; and (3) by hydrogen bonding with the y-phosphate. The structural resemblance with carbamate kinase and the alignment of the sequences suggest that NAGK is a structural and functional prototype for the amino acid kinase family, which differs from other acylphosphate-making devices represented by phosphoglycerate kinase, acetate kinase, and biotin carboxylase. | ||
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- | Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis.,Ramon-Maiques S, Marina A, Gil-Ortiz F, Fita I, Rubio V Structure. 2002 Mar;10(3):329-42. PMID:12005432<ref>PMID:12005432</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1gsj" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Acetylglutamate kinase]] | ||
- | [[Category: Ecobd]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Fita | + | [[Category: Fita I]] |
- | [[Category: Gil-Ortiz | + | [[Category: Gil-Ortiz F]] |
- | [[Category: Marina | + | [[Category: Marina A]] |
- | [[Category: Ramon-Maiques | + | [[Category: Ramon-Maiques S]] |
- | [[Category: Rubio | + | [[Category: Rubio V]] |
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Current revision
Selenomethionine substituted N-acetyl-L-glutamate kinase from Escherichia coli complexed with its substrate n-acetyl-L-glutamate and its substrate analog AMPPNP
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