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[[Image:1moh.gif|left|200px]]
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{{STRUCTURE_1moh|  PDB=1moh  |  SCENE=  }}
'''FERRIC MONOMERIC HEMOGLOBIN I (HB I)'''


==FERRIC MONOMERIC HEMOGLOBIN I (HB I)==
<StructureSection load='1moh' size='340' side='right'caption='[[1moh]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1moh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phacoides_pectinatus Phacoides pectinatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MOH 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</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=1moh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1moh OCA], [https://pdbe.org/1moh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1moh RCSB], [https://www.ebi.ac.uk/pdbsum/1moh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1moh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLB1_PHAPT GLB1_PHAPT] Serves to transport hydrogen sulfide to autotrophic bacteria.
== 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/mo/1moh_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=1moh ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The X-ray crystal structure of the sulfide derivative of ferric Lucina pectinata hemoglobin component I (HbI) has been determined at 1.9 A resolution (R-factor 0.186). The heme pocket structural organization of HbI is in keeping with its ligand binding properties. The fast sulfide association rate constant can be related to the presence of Gln(64)E7, as the heme distal residue, together with the protein structural properties in the CD-E distal region. Moreover, the very high sulfide affinity for HbI is reflected by the exceptionally slow ligand dissociation rate. The stabilization of the heme-bound sulfide molecule is achieved through hydrogen bonding to Gln(64)E7, as well as by finely tuned aromatic-electrostatic interactions with the clustered residues Phe(29)B10, Phe(43)CD1 and Phe(68)E11. Such a peculiar arrangement of phenylalanyl residues at the distal ligand binding site has not been observed before in the globin family, and is unique to HbI, a protein functionally devoted to sulfide transport.


==Overview==
Structural bases for sulfide recognition in Lucina pectinata hemoglobin I.,Rizzi M, Wittenberg JB, Coda A, Ascenzi P, Bolognesi M J Mol Biol. 1996 Apr 26;258(1):1-5. PMID:8613980<ref>PMID:8613980</ref>
The X-ray crystal structure of the sulfide derivative of ferric Lucina pectinata hemoglobin component I (HbI) has been determined at 1.9 A resolution (R-factor 0.186). The heme pocket structural organization of HbI is in keeping with its ligand binding properties. The fast sulfide association rate constant can be related to the presence of Gln(64)E7, as the heme distal residue, together with the protein structural properties in the CD-E distal region. Moreover, the very high sulfide affinity for HbI is reflected by the exceptionally slow ligand dissociation rate. The stabilization of the heme-bound sulfide molecule is achieved through hydrogen bonding to Gln(64)E7, as well as by finely tuned aromatic-electrostatic interactions with the clustered residues Phe(29)B10, Phe(43)CD1 and Phe(68)E11. Such a peculiar arrangement of phenylalanyl residues at the distal ligand binding site has not been observed before in the globin family, and is unique to HbI, a protein functionally devoted to sulfide transport.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1MOH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lucina_pectinata Lucina pectinata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOH OCA].
</div>
<div class="pdbe-citations 1moh" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural bases for sulfide recognition in Lucina pectinata hemoglobin I., Rizzi M, Wittenberg JB, Coda A, Ascenzi P, Bolognesi M, J Mol Biol. 1996 Apr 26;258(1):1-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8613980 8613980]
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
[[Category: Lucina pectinata]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Ascenzi, P.]]
__TOC__
[[Category: Bolognesi, M.]]
</StructureSection>
[[Category: Rizzi, M.]]
[[Category: Large Structures]]
[[Category: Wittenberg, J B.]]
[[Category: Phacoides pectinatus]]
[[Category: Monomeric]]
[[Category: Ascenzi P]]
[[Category: Sulfide transport]]
[[Category: Bolognesi M]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:31:23 2008''
[[Category: Rizzi M]]
[[Category: Wittenberg JB]]
Retrieved from "https://proteopedia.org/1moh"