3nok: Difference between revisions

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-{{Seed}}
-[[Image:3nok.jpg|left|200px]]
-<!--
+==Crystal structure of Myxococcus xanthus Glutaminyl Cyclase==
-The line below this paragraph, containing "STRUCTURE_3nok", creates the "Structure Box" on the page.
+<StructureSection load='3nok' size='340' side='right'caption='[[3nok]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3nok]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NOK FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DDQ:DECYLAMINE-N,N-DIMETHYL-N-OXIDE'>DDQ</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
-{{STRUCTURE_3nok|  PDB=3nok  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3nok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nok OCA], [https://pdbe.org/3nok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nok RCSB], [https://www.ebi.ac.uk/pdbsum/3nok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nok ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/E7FH78_MYXXA E7FH78_MYXXA]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Abstract Although enzymes responsible for the cyclization of amino terminal glutamine residues are present in both plant and mammal species, none have yet been characterized in bacteria. Based on low sequence homologies to plant glutaminyl cyclases (QC), we cloned the coding sequences of putative microbial QCs from Zymomonas mobilis (ZmQC) and Myxococcus xanthus (MxQC). The two recombinant enzymes exhibited distinct QC activity, with specificity constants k(cat)/K(m) of 1.47+/-0.33 mm(-1)s(-1) (ZmQC) and 142+/-32.7 mm(-1)s(-1) (MxQC) towards the fluorescent substrate glutamine-7-amino-4-methyl-coumarine. The measured pH-rate profile of the second order rate constant displayed an interesting deviation towards the acidic limb of the pH chart in the case of ZmQC, while MxQC showed maximum activity in the mild alkaline pH range. Analysis of the enzyme variants ZmQCGlu(46)Gln and MxQCGln(46)Glu show that the exchanged residues play a significant role in the pH behaviour of the respective enzymes. In addition, we determined the three dimensional crystal structures of both enzymes. The tertiary structure is defined by a five-bladed beta-propeller anchored by a core cation. The structures corroborate the putative location of the active site and confirm the proposed relationship between bacterial and plant glutaminyl cyclases.
-===Crystal structure of Myxococcus xanthus Glutaminyl Cyclase===
+Kinetic and structural characterization of bacterial glutaminyl cyclases from Zymomonas mobilis and Myxococcus xanthus.,Carrillo DR, Parthier C, Janckel N, Grandke J, Stelter M, Schilling S, Boehme M, Neumann P, Wolf R, Demuth HU, Stubbs MT, Rahfeld JU Biol Chem. 2010 Sep 24. PMID:20868223<ref>PMID:20868223</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3nok" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_20868223}}, adds the Publication Abstract to the page
+*[[Glutaminyl cyclase|Glutaminyl cyclase]]
-(as it appears on PubMed at http://www.pubmed.gov), where 20868223 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_20868223}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-NOK is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NOK OCA].
-==Reference==
-<ref group="xtra">PMID:20868223</ref><references group="xtra"/>
-[[Category: Glutaminyl-peptide cyclotransferase]]
 [[Category: Myxococcus xanthus]]
-[[Category: Carrillo, D R.]]
+[[Category: Carrillo DR]]
-[[Category: Parthier, C.]]
+[[Category: Parthier C]]
-[[Category: Stubbs, M T.]]
+[[Category: Stubbs MT]]
-[[Category: Beta-propeller]]
-[[Category: Cyclotransferase]]
-[[Category: Glutaminyl cyclase]]
-[[Category: Pyroglutamate]]
-[[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov  3 11:11:45 2010''