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==APPLICATION OF AN AUTOMATIC MOLECULAR REPLACEMENT PROCEDURE TO CRYSTAL STRUCTURE OF CYTOCHROME C2 FROM RHODOPSEUDOMONAS VIRIDIS==
==APPLICATION OF AN AUTOMATIC MOLECULAR REPLACEMENT PROCEDURE TO CRYSTAL STRUCTURE OF CYTOCHROME C2 FROM RHODOPSEUDOMONAS VIRIDIS==
<StructureSection load='1cry' size='340' side='right' caption='[[1cry]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='1cry' size='340' side='right'caption='[[1cry]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1cry]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CRY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CRY FirstGlance]. <br>
<table><tr><td colspan='2'>[[1cry]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Blastochloris_viridis Blastochloris viridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CRY FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 3&#8491;</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=1cry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cry OCA], [http://pdbe.org/1cry PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cry RCSB], [http://www.ebi.ac.uk/pdbsum/1cry PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cry ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</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=1cry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cry OCA], [https://pdbe.org/1cry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cry RCSB], [https://www.ebi.ac.uk/pdbsum/1cry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cry ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CYC2_BLAVI CYC2_BLAVI]] Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria.  
[https://www.uniprot.org/uniprot/CYC2_BLAVI CYC2_BLAVI] Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cr/1cry_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cr/1cry_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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==See Also==
==See Also==
*[[Cytochrome c|Cytochrome c]]
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Miki, K]]
[[Category: Blastochloris viridis]]
[[Category: Sogabe, S]]
[[Category: Large Structures]]
[[Category: Miki K]]
[[Category: Sogabe S]]

Latest revision as of 10:13, 9 October 2024

APPLICATION OF AN AUTOMATIC MOLECULAR REPLACEMENT PROCEDURE TO CRYSTAL STRUCTURE OF CYTOCHROME C2 FROM RHODOPSEUDOMONAS VIRIDISAPPLICATION OF AN AUTOMATIC MOLECULAR REPLACEMENT PROCEDURE TO CRYSTAL STRUCTURE OF CYTOCHROME C2 FROM RHODOPSEUDOMONAS VIRIDIS

Structural highlights

1cry is a 1 chain structure with sequence from Blastochloris viridis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CYC2_BLAVI Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic 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

An automatic molecular-replacement procedure has been applied to solve the crystal structure of cytochrome c(2) from Rhodopseudomonas viridis. The structure was solved on the basis of the structure of tuna cytochrome c as a search model using an automatic processing program system, AUTOMR. The refinements by molecular dynamics and restrained least-squares methods result in a current crystallographic R factor of 0.219 for diffraction data at 3 A resolution.

Application of an automatic molecular-replacement procedure to crystal structure analysis of cytochrome c2 from Rhodopseudomonas viridis.,Miki K, Sogabe S, Uno A, Ezoe T, Kasai N, Saeda M, Matsuura Y, Miki M Acta Crystallogr D Biol Crystallogr. 1994 May 1;50(Pt 3):271-5. PMID:15299438[1]

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

See Also

References

  1. Miki K, Sogabe S, Uno A, Ezoe T, Kasai N, Saeda M, Matsuura Y, Miki M. Application of an automatic molecular-replacement procedure to crystal structure analysis of cytochrome c2 from Rhodopseudomonas viridis. Acta Crystallogr D Biol Crystallogr. 1994 May 1;50(Pt 3):271-5. PMID:15299438 doi:10.1107/S0907444993013952

1cry, resolution 3.00Å

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OCA