1mfz
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1mfz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mfz, resolution 2.8Å" /> '''Partially refined 2.8...) |
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- | [[Image:1mfz.gif|left|200px]]<br /><applet load="1mfz" size="450" color="white" frame="true" align="right" spinBox="true" | ||
- | caption="1mfz, resolution 2.8Å" /> | ||
- | '''Partially refined 2.8 A Crystal structure of GDP-mannose dehydrogenase from P. aeruginosa'''<br /> | ||
- | == | + | ==Partially refined 2.8 A Crystal structure of GDP-mannose dehydrogenase from P. aeruginosa== |
- | The enzyme GMD from Pseudomonas aeruginosa catalyzes the committed step in | + | <StructureSection load='1mfz' size='340' side='right'caption='[[1mfz]], [[Resolution|resolution]] 2.80Å' scene=''> |
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1mfz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MFZ FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDX:GUANOSINE+5-(TRIHYDROGEN+DIPHOSPHATE),+P-D-MANNOPYRANOSYL+ESTER'>GDX</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1mfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mfz OCA], [https://pdbe.org/1mfz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mfz RCSB], [https://www.ebi.ac.uk/pdbsum/1mfz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mfz ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/ALGD_PSEAE ALGD_PSEAE] Catalyzes the oxidation of guanosine diphospho-D-mannose (GDP-D-mannose) to GDP-D-mannuronic acid, a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mf/1mfz_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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=1mfz ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The enzyme GMD from Pseudomonas aeruginosa catalyzes the committed step in the synthesis of the exopolysaccharide alginate. Alginate is a major component of P. aeruginosa biofilms that protect the bacteria from the host immune response and antibiotic therapy. The 1.55 A crystal structure of GMD in ternary complex with its cofactor NAD(H) and product GDP-mannuronic acid reveals that the enzyme forms a domain-swapped dimer with two polypeptide chains contributing to each active site. The extensive dimer interface provides multiple opportunities for intersubunit communication. Comparison of the GMD structure with that of UDP-glucose dehydrogenase reveals the structural basis of sugar binding specificity that distinguishes these two related enzyme families. The high-resolution structure of GMD provides detailed information on the active site of the enzyme and a template for structure-based inhibitor design. | ||
- | + | Crystal structure of GDP-mannose dehydrogenase: a key enzyme of alginate biosynthesis in P. aeruginosa.,Snook CF, Tipton PA, Beamer LJ Biochemistry. 2003 Apr 29;42(16):4658-68. PMID:12705829<ref>PMID:12705829</ref> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | [[Category: | + | <div class="pdbe-citations 1mfz" style="background-color:#fffaf0;"></div> |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
- | + | [[Category: Beamer LJ]] | |
- | [[Category: Beamer | + | [[Category: Snook CF]] |
- | [[Category: Snook | + | [[Category: Tipton PA]] |
- | [[Category: Tipton | + | |
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Current revision
Partially refined 2.8 A Crystal structure of GDP-mannose dehydrogenase from P. aeruginosa
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