3tm9: Difference between revisions

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 <StructureSection load='3tm9' size='340' side='right'caption='[[3tm9]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3tm9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_15218 Atcc 15218]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TM9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3tm9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vitreoscilla_stercoraria Vitreoscilla stercoraria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TM9 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vhb|2vhb]], [[3tld|3tld]], [[3tm3|3tm3]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">vhb ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=61 ATCC 15218])</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=3tm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tm9 OCA], [https://pdbe.org/3tm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tm9 RCSB], [https://www.ebi.ac.uk/pdbsum/3tm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tm9 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/BAHG_VITST BAHG_VITST]] This protein functions as a terminal oxidase.
+[https://www.uniprot.org/uniprot/BAHG_VITST BAHG_VITST] This protein functions as a terminal oxidase.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Site-directed mutants of the gene encoding wild-type Vitreoscilla hemoglobin were made that changed Tyr29 (B10) of the wild-type Vitreoscilla hemoglobin (VHb) to either Phe or Ala. The wild-type and the two mutant hemoglobins were expressed in Escherichia coli and purified to homogeneity. The binding of the two mutants to CO was essentially identical to that of wild-type VHb as determined by CO-difference spectra. Circular-dichroism spectra also showed the two mutants to be essentially the same as wild-type VHb regarding overall helicity. All three VHbs were crystallized and their structures were determined at resolutions of 1.7-1.9 A, which are similar to that of the original wild-type structure determination. The Tyr29Phe mutant has a structure that is essentially indistinguishable from that of the wild type. However, the structure of the Tyr29Ala mutant has significant differences from that of the wild type. In addition, for the Tyr29Ala mutant it was possible to determine the positions of most of the residues in the D region, which was disordered in the originally reported structure of wild-type VHb as well as in the wild-type VHb structure reported here. In the Tyr29Ala mutant, the five-membered ring of proline E8 (Pro54) occupies the space occupied by the aromatic ring of Tyr29 in the wild-type structure. These results are discussed in the context of the proposed role of Tyr29 in the structure of the oxygen-binding pocket.
-Crystallographic structure determination of B10 mutants of Vitreoscilla hemoglobin: role of Tyr29 (B10) in the structure of the ligand-binding site.,Ratakonda S, Anand A, Dikshit K, Stark BC, Howard AJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Mar 1;69(Pt 3):215-22., doi: 10.1107/S1744309112044818. Epub 2013 Feb 22. PMID:23519792<ref>PMID:23519792</ref>
+==See Also==
+*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3tm9" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 15218]]
 [[Category: Large Structures]]
-[[Category: Anand, A]]
+[[Category: Vitreoscilla stercoraria]]
-[[Category: Dikshit, K]]
+[[Category: Anand A]]
-[[Category: Howard, A J]]
+[[Category: Dikshit K]]
-[[Category: Ratakonda, S]]
+[[Category: Howard AJ]]
-[[Category: Stark, B C]]
+[[Category: Ratakonda S]]
-[[Category: Globin 8-helix fold]]
+[[Category: Stark BC]]
-[[Category: Oxygen storage]]
-[[Category: Oxygen transport]]