1ux8

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[[Image:1ux8.jpg|left|200px]]
 
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==X-ray structure of truncated oxygen-avid haemoglobin from Bacillus subtilis==
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The line below this paragraph, containing "STRUCTURE_1ux8", creates the "Structure Box" on the page.
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<StructureSection load='1ux8' size='340' side='right'caption='[[1ux8]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ux8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UX8 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.15&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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{{STRUCTURE_1ux8| PDB=1ux8 | SCENE= }}
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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=1ux8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ux8 OCA], [https://pdbe.org/1ux8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ux8 RCSB], [https://www.ebi.ac.uk/pdbsum/1ux8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ux8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRHBO_BACSU TRHBO_BACSU] Hemoglobin-like protein that exhibits a low peroxidase activity. Its very high oxygen affinity may rule out the possibility that it is involved in oxygen transport.<ref>PMID:15866723</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ux/1ux8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ux8 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The group II truncated hemoglobin from Bacillus subtilis has been cloned, expressed, purified, and characterized. B. subtilis truncated hemoglobin is a monomeric protein endowed with an unusually high oxygen affinity (in the nanomolar range) such that the apparent thermodynamic binding constant for O2 exceeds that for CO by 1 order of magnitude. The kinetic basis of the high oxygen affinity resides mainly in the very slow rate of ligand release. The extremely stable ferrous oxygenated adduct is resistant to oxidation, which can be achieved only with oxidant in large excess, e.g. ferricyanide in 50-fold molar excess. The three-dimensional crystal structure of the cyano-Met derivative was determined at 2.15 A resolution. Although the overall fold resembles that of other truncated hemoglobins, the distal heme pocket displays a unique array of hydrophilic side chains in the topological positions that dominate the steric interaction with iron-bound ligands. In fact, the Tyr-B10, Thr-E7, and Gln-E11 oxygens on one side of the heme pocket and the Trp-G8 indole NE1 nitrogen on the other form a novel pattern of the "ligand-inclusive hydrogen bond network" described for mycobacterial HbO. On the proximal side, the histidine residue is in an unstrained conformation, and the iron-His bond is unusually short (1.91 A).
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'''X-RAY STRUCTURE OF TRUNCATED OXYGEN-AVID HAEMOGLOBIN FROM BACILLUS SUBTILIS'''
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The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray structure and ligand binding properties.,Giangiacomo L, Ilari A, Boffi A, Morea V, Chiancone E J Biol Chem. 2005 Mar 11;280(10):9192-202. Epub 2004 Dec 7. PMID:15590662<ref>PMID:15590662</ref>
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==Overview==
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The group II truncated hemoglobin from Bacillus subtilis has been cloned, expressed, purified, and characterized. B. subtilis truncated hemoglobin is a monomeric protein endowed with an unusually high oxygen affinity (in the nanomolar range) such that the apparent thermodynamic binding constant for O2 exceeds that for CO by 1 order of magnitude. The kinetic basis of the high oxygen affinity resides mainly in the very slow rate of ligand release. The extremely stable ferrous oxygenated adduct is resistant to oxidation, which can be achieved only with oxidant in large excess, e.g. ferricyanide in 50-fold molar excess. The three-dimensional crystal structure of the cyano-Met derivative was determined at 2.15 A resolution. Although the overall fold resembles that of other truncated hemoglobins, the distal heme pocket displays a unique array of hydrophilic side chains in the topological positions that dominate the steric interaction with iron-bound ligands. In fact, the Tyr-B10, Thr-E7, and Gln-E11 oxygens on one side of the heme pocket and the Trp-G8 indole NE1 nitrogen on the other form a novel pattern of the "ligand-inclusive hydrogen bond network" described for mycobacterial HbO. On the proximal side, the histidine residue is in an unstrained conformation, and the iron-His bond is unusually short (1.91 A).
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1UX8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UX8 OCA].
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</div>
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<div class="pdbe-citations 1ux8" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray structure and ligand binding properties., Giangiacomo L, Ilari A, Boffi A, Morea V, Chiancone E, J Biol Chem. 2005 Mar 11;280(10):9192-202. Epub 2004 Dec 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15590662 15590662]
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*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Boffi, A.]]
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[[Category: Boffi A]]
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[[Category: Chiancone, E.]]
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[[Category: Chiancone E]]
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[[Category: Giangiacomo, L.]]
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[[Category: Giangiacomo L]]
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[[Category: Ilari, A.]]
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[[Category: Ilari A]]
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[[Category: Oxygen transport]]
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[[Category: Truncated hemoglobin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:48:29 2008''
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Current revision

X-ray structure of truncated oxygen-avid haemoglobin from Bacillus subtilis

PDB ID 1ux8

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