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[[Image:1vre.gif|left|200px]]
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{{STRUCTURE_1vre|  PDB=1vre  |  SCENE=  }}
'''SOLUTION STRUCTURE OF COMPONENT IV GLYCERA DIBRANCHIATA MONOMERIC HEMOGLOBIN-CO'''


==SOLUTION STRUCTURE OF COMPONENT IV GLYCERA DIBRANCHIATA MONOMERIC HEMOGLOBIN-CO==
<StructureSection load='1vre' size='340' side='right'caption='[[1vre]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1vre]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycera_dibranchiata Glycera dibranchiata]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VRE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR,  models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</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=1vre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vre OCA], [https://pdbe.org/1vre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vre RCSB], [https://www.ebi.ac.uk/pdbsum/1vre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vre ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLB4_GLYDI GLB4_GLYDI]
== 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/vr/1vre_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=1vre ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The solution structure and backbone dynamics of the recombinant, ferrous CO-ligated form of component IV monomeric hemoglobin from Glycera dibranchiata (GMH4CO) have been characterized by NMR spectroscopy. Distance geometry and simulated annealing calculations utilizing a total of 2550 distance and torsion angle constraints yielded an ensemble of 29 structures with an overall average backbone rmsd of 0.48 A from the average structure. Differences between the solution structure and a related crystal structure are confined to regions of lower precision in either the NMR or X-ray structure, or in regions where the amino acid sequences differ. 15N relaxation measurements at 76.0 and 60.8 MHz were analyzed with an extended model-free approach, and revealed low-frequency motions in the vicinity of the heme, concentrated in the F helix. Amide proton protection factors were obtained from H-D amide exchange measurements on 15N-labeled protein. Patterns in the backbone dynamics and protection factors were shown to correlate with regions of heterogeneity and disorder in the ensemble of NMR structures and with large crystallographic B-factors in the X-ray structures. Surprisingly, while the backbone atoms of the F helix have higher rmsds and larger measures of dynamics on the microsecond to millisecond time scale than the other helices, amide protection factors for residues in the F helix were observed to be similar to those of the other helices. This contrasts with H-D amide exchange measurements on sperm whale myoglobin which indicated low protection for the F helix (S. N. Loh and B. F. Volkman, unpublished results). These results for GMH4 suggest a model in which the F helix undergoes collective motions as a relatively rigid hydrogen-bonded unit, possibly pivoting about a central position near residue Val87.


==Overview==
Solution structure and backbone dynamics of component IV Glycera dibranchiata monomeric hemoglobin-CO.,Volkman BF, Alam SL, Satterlee JD, Markley JL Biochemistry. 1998 Aug 4;37(31):10906-19. PMID:9692983<ref>PMID:9692983</ref>
The solution structure and backbone dynamics of the recombinant, ferrous CO-ligated form of component IV monomeric hemoglobin from Glycera dibranchiata (GMH4CO) have been characterized by NMR spectroscopy. Distance geometry and simulated annealing calculations utilizing a total of 2550 distance and torsion angle constraints yielded an ensemble of 29 structures with an overall average backbone rmsd of 0.48 A from the average structure. Differences between the solution structure and a related crystal structure are confined to regions of lower precision in either the NMR or X-ray structure, or in regions where the amino acid sequences differ. 15N relaxation measurements at 76.0 and 60.8 MHz were analyzed with an extended model-free approach, and revealed low-frequency motions in the vicinity of the heme, concentrated in the F helix. Amide proton protection factors were obtained from H-D amide exchange measurements on 15N-labeled protein. Patterns in the backbone dynamics and protection factors were shown to correlate with regions of heterogeneity and disorder in the ensemble of NMR structures and with large crystallographic B-factors in the X-ray structures. Surprisingly, while the backbone atoms of the F helix have higher rmsds and larger measures of dynamics on the microsecond to millisecond time scale than the other helices, amide protection factors for residues in the F helix were observed to be similar to those of the other helices. This contrasts with H-D amide exchange measurements on sperm whale myoglobin which indicated low protection for the F helix (S. N. Loh and B. F. Volkman, unpublished results). These results for GMH4 suggest a model in which the F helix undergoes collective motions as a relatively rigid hydrogen-bonded unit, possibly pivoting about a central position near residue Val87.


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


==Reference==
==See Also==
Solution structure and backbone dynamics of component IV Glycera dibranchiata monomeric hemoglobin-CO., Volkman BF, Alam SL, Satterlee JD, Markley JL, Biochemistry. 1998 Aug 4;37(31):10906-19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9692983 9692983]
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Glycera dibranchiata]]
[[Category: Glycera dibranchiata]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Alam, S L.]]
[[Category: Alam SL]]
[[Category: Markley, J L.]]
[[Category: Markley JL]]
[[Category: Satterlee, J D.]]
[[Category: Satterlee JD]]
[[Category: Volkman, B F.]]
[[Category: Volkman BF]]
[[Category: Globin]]
[[Category: Heme protein]]
[[Category: Oxygen transport]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 12:50:02 2008''
Retrieved from "https://proteopedia.org/1vre"