|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='1ux8' size='340' side='right'caption='[[1ux8]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='1ux8' size='340' side='right'caption='[[1ux8]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ux8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UX8 FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ux8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ux8 OCA], [http://pdbe.org/1ux8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ux8 RCSB], [http://www.ebi.ac.uk/pdbsum/1ux8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ux8 ProSAT]</span></td></tr> | + | <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> |
| | + | <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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 35: |
Line 36: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Boffi, A]] | + | [[Category: Boffi A]] |
| - | [[Category: Chiancone, E]] | + | [[Category: Chiancone E]] |
| - | [[Category: Giangiacomo, L]] | + | [[Category: Giangiacomo L]] |
| - | [[Category: Ilari, A]] | + | [[Category: Ilari A]] |
| - | [[Category: Oxygen storage-transport complex]]
| + | |
| - | [[Category: Oxygen storage/transport]]
| + | |
| - | [[Category: Oxygen transport]]
| + | |
| - | [[Category: Truncated hemoglobin]]
| + | |
| Structural highlights
Function
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.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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).
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Choudhary ML, Jawaid S, Ahuja MK, Shiva NK, Gupta P, Bhuyan AK, Khatri GS. Open reading frame yjbI of Bacillus subtilis codes for truncated hemoglobin. Protein Expr Purif. 2005 Jun;41(2):363-72. PMID:15866723 doi:http://dx.doi.org/S1046-5928(05)00077-X
- ↑ Giangiacomo L, Ilari A, Boffi A, Morea V, Chiancone E. The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray structure and ligand binding properties. J Biol Chem. 2005 Mar 11;280(10):9192-202. Epub 2004 Dec 7. PMID:15590662 doi:10.1074/jbc.M407267200
|
