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1moh

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Revision as of 06:54, 25 August 2021

FERRIC MONOMERIC HEMOGLOBIN I (HB I)

Structural highlights

1moh is a 1 chain structure with sequence from Lucina pectinata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GLB1_PHAPT] Serves to transport hydrogen sulfide to autotrophic bacteria.

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 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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rizzi M, Wittenberg JB, Coda A, Ascenzi P, Bolognesi M. Structural bases for sulfide recognition in Lucina pectinata hemoglobin I. J Mol Biol. 1996 Apr 26;258(1):1-5. PMID:8613980 doi:http://dx.doi.org/10.1006/jmbi.1996.0228

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1moh"

@@ Line 3: / Line 3: @@
 <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 [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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1moh]] is a 1 chain structure with sequence from [https://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]. 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
+</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1moh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1moh OCA], [http://pdbe.org/1moh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1moh RCSB], [http://www.ebi.ac.uk/pdbsum/1moh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1moh ProSAT]</span></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 ==
-[[http://www.uniprot.org/uniprot/GLB1_PHAPT GLB1_PHAPT]] Serves to transport hydrogen sulfide to autotrophic bacteria.
+[[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]]

1moh

From Proteopedia

Revision as of 06:54, 25 August 2021

FERRIC MONOMERIC HEMOGLOBIN I (HB I)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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