1bvc: Difference between revisions

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New page: left|200px<br /><applet load="1bvc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bvc, resolution 1.5Å" /> '''STRUCTURE OF A BILIVE...
 
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[[Image:1bvc.gif|left|200px]]<br /><applet load="1bvc" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1bvc, resolution 1.5&Aring;" />
'''STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM D) AT 118 K'''<br />


==Overview==
==STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM D) AT 118 K==
Crystal structure determinations of two orthorhombic (P2(1)2(1)2(1)), crystal modifications of the biliverdin apomyoglobin complex are, described. The two structures were determined by X-ray diffraction at 100, K to a resolution of 1.5 A and 1.4 A. Both crystal forms were grown by, hanging-drop techniques, using phosphate as precipitant. The structures, were solved by molecular replacement and refined to final R-values of, 19.4% and 21.2%. Both structures are very similar with respect to the, binding site and the conformation of the biliverdin chromophore, which, occurs in a (P) helical conformation. It is located within the heme, pocket, very close in position and orientation to the heme binding site in, myoglobin. Two water molecules not present in the crystal structure of, myoglobin are sequestered within the heme pocket in the, biliverdin-apomyoglobin complex, and they are engaged in hydrogen bonding, to the biliverdin and to the protein. Comparison with structural results, from an earlier NMR study of the same complex shows good agreement.
<StructureSection load='1bvc' size='340' side='right'caption='[[1bvc]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bvc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BVC 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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BLA:BILIVERDINE+IX+ALPHA'>BLA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1bvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bvc OCA], [https://pdbe.org/1bvc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bvc RCSB], [https://www.ebi.ac.uk/pdbsum/1bvc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bvc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
== 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/bv/1bvc_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1bvc ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1BVC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with PO4 and BLA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BVC OCA].
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structure determination of the biliverdin apomyoglobin complex: crystal structure analysis of two crystal forms at 1.4 and 1.5 A resolution., Wagner UG, Muller N, Schmitzberger W, Falk H, Kratky C, J Mol Biol. 1995 Mar 24;247(2):326-37. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7707378 7707378]
[[Category: Large Structures]]
[[Category: Physeter catodon]]
[[Category: Physeter catodon]]
[[Category: Single protein]]
[[Category: Falk H]]
[[Category: Falk, H.]]
[[Category: Kratky C]]
[[Category: Kratky, C.]]
[[Category: Mueller N]]
[[Category: Mueller, N.]]
[[Category: Schmitzberger W]]
[[Category: Schmitzberger, W.]]
[[Category: Wagner UG]]
[[Category: Wagner, U.G.]]
[[Category: BLA]]
[[Category: PO4]]
[[Category: oxygen storage]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:56:59 2007''

Latest revision as of 09:39, 7 February 2024

STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM D) AT 118 KSTRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM D) AT 118 K

Structural highlights

1bvc is a 1 chain structure with sequence from Physeter catodon. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MYG_PHYMC Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1bvc, resolution 1.50Å

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