3s7y

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Current revision (12:49, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3s7y' size='340' side='right'caption='[[3s7y]], [[Resolution|resolution]] 4.31&Aring;' scene=''>
<StructureSection load='3s7y' size='340' side='right'caption='[[3s7y]], [[Resolution|resolution]] 4.31&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3s7y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Marmm Marmm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S7Y FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3s7y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Maricaulis_maris_MCS10 Maricaulis maris MCS10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S7Y FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3s6g|3s6g]], [[3s6h|3s6h]], [[3s6k|3s6k]]</div></td></tr>
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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]] 4.3077&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">argA/B, Mmar10_0365 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=394221 MARMM])</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=3s7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s7y OCA], [https://pdbe.org/3s7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s7y RCSB], [https://www.ebi.ac.uk/pdbsum/3s7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s7y 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=3s7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s7y OCA], [https://pdbe.org/3s7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s7y RCSB], [https://www.ebi.ac.uk/pdbsum/3s7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s7y ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q0ASS9_MARMM Q0ASS9_MARMM]
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Novel bifunctional N-acetylglutamate synthase/kinases (NAGS/K) that catalyze the first two steps of arginine biosynthesis and are homologous to vertebrate N-acetylglutamate synthase (NAGS), an essential cofactor-producing enzyme in the urea cycle, were identified in Maricaulis maris and several other bacteria. Arginine is an allosteric inhibitor of NAGS but not NAGK activity. The crystal structure of M. maris NAGS/K (mmNAGS/K) at 2.7 A resolution indicates that it is a tetramer, in contrast to the hexameric structure of Neisseria gonorrhoeae NAGS. The quaternary structure of crystalline NAGS/K from Xanthomonas campestris (xcNAGS/K) is similar, and cross-linking experiments indicate that both mmNAGS/K and xcNAGS are tetramers in solution. Each subunit has an amino acid kinase (AAK) domain, which is likely responsible for N-acetylglutamate kinase (NAGK) activity and has a putative arginine binding site, and an N-acetyltransferase (NAT) domain that contains the putative NAGS active site. These structures and sequence comparisons suggest that the linker residue 291 may determine whether arginine acts as an allosteric inhibitor or activator in homologous enzymes in microorganisms and vertebrates. In addition, the angle of rotation between AAK and NAT domains varies among crystal forms and subunits within the tetramer. A rotation of 26 degrees is sufficient to close the predicted AcCoA binding site, thus reducing enzymatic activity. Since mmNAGS/K has the highest degree of sequence homology to vertebrate NAGS of NAGS and NAGK enzymes whose structures have been determined, the mmNAGS/K structure was used to develop a structural model of human NAGS that is fully consistent with the functional effects of the 14 missense mutations that were identified in NAGS-deficient patients.
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A Novel N-acetylglutamate synthase architecture revealed by the crystal structure of the bifunctional enzyme from Maricaulis maris.,Shi D, Li Y, Cabrera-Luque J, Jin Z, Yu X, Zhao G, Haskins N, Allewell NM, Tuchman M PLoS One. 2011;6(12):e28825. Epub 2011 Dec 12. PMID:22174908<ref>PMID:22174908</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3s7y" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Marmm]]
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[[Category: Maricaulis maris MCS10]]
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[[Category: Allewell, N M]]
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[[Category: Allewell NM]]
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[[Category: Cabrera-Luque, J]]
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[[Category: Cabrera-Luque J]]
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[[Category: Jin, Z]]
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[[Category: Jin Z]]
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[[Category: Li, Y]]
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[[Category: Li Y]]
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[[Category: Shi, D]]
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[[Category: Shi D]]
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[[Category: Tuchman, M]]
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[[Category: Tuchman M]]
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[[Category: Yu, X]]
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[[Category: Yu X]]
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[[Category: Kinase]]
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[[Category: Synthase]]
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[[Category: Transferase]]
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Current revision

Crystal structure of mmNAGS in Space Group P3121 at 4.3 A resolution

PDB ID 3s7y

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