1r1n
From Proteopedia
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| - | [[Image:1r1n.gif|left|200px]]<br /><applet load="1r1n" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1r1n, resolution 1.74Å" /> | ||
| - | '''Tri-nuclear oxo-iron clusters in the ferric binding protein from N. gonorrhoeae'''<br /> | ||
| - | == | + | ==Tri-nuclear oxo-iron clusters in the ferric binding protein from N. gonorrhoeae== |
| + | <StructureSection load='1r1n' size='340' side='right'caption='[[1r1n]], [[Resolution|resolution]] 1.74Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1r1n]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R1N 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]] 1.74Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CN1:OXO-IRON+CLUSTER+2'>CN1</scene>, <scene name='pdbligand=CNB:OXO-IRON+CLUSTER+1'>CNB</scene>, <scene name='pdbligand=CNF:OXO-IRON+CLUSTER+3'>CNF</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=1r1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r1n OCA], [https://pdbe.org/1r1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r1n RCSB], [https://www.ebi.ac.uk/pdbsum/1r1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r1n ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FBP_NEIGO FBP_NEIGO] This protein may be a central component in the iron-acquisition system. | ||
| + | == 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/r1/1r1n_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=1r1n ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
We report a set of three 1.8-1.9 A resolution X-ray crystal structures of Neisseria gonorrhoeae Fbp (ferric-ion binding protein): (i) open-cleft apo-Fbp containing bound phosphate, (ii) open-cleft mono-Fe Fbp capped by nitrilotriacetate, and (iii) open-cleft trinuclear oxo-iron Fbp, the first structure of an iron-cluster adduct of a transferrin. The nine independent molecules in the unit cells provide 'snapshots' of the versatile dynamic structural roles of the conserved dityrosyl iron-binding motif (Tyr195-Tyr196) which control the capture and, possibly, processing of iron. These findings have implications for understanding bacterial iron acquisition and dissimilation, and organic/mineral interfaces. | We report a set of three 1.8-1.9 A resolution X-ray crystal structures of Neisseria gonorrhoeae Fbp (ferric-ion binding protein): (i) open-cleft apo-Fbp containing bound phosphate, (ii) open-cleft mono-Fe Fbp capped by nitrilotriacetate, and (iii) open-cleft trinuclear oxo-iron Fbp, the first structure of an iron-cluster adduct of a transferrin. The nine independent molecules in the unit cells provide 'snapshots' of the versatile dynamic structural roles of the conserved dityrosyl iron-binding motif (Tyr195-Tyr196) which control the capture and, possibly, processing of iron. These findings have implications for understanding bacterial iron acquisition and dissimilation, and organic/mineral interfaces. | ||
| - | + | Oxo-iron clusters in a bacterial iron-trafficking protein: new roles for a conserved motif.,Zhu H, Alexeev D, Hunter DJ, Campopiano DJ, Sadler PJ Biochem J. 2003 Nov 15;376(Pt 1):35-41. PMID:13129433<ref>PMID:13129433</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1r1n" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Ferric-binding protein|Ferric-binding protein]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Neisseria gonorrhoeae]] | ||
| + | [[Category: Alexeev D]] | ||
| + | [[Category: Campopiano DJ]] | ||
| + | [[Category: Hunter DJ]] | ||
| + | [[Category: Sadler PJ]] | ||
| + | [[Category: Zhu H]] | ||
Current revision
Tri-nuclear oxo-iron clusters in the ferric binding protein from N. gonorrhoeae
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