1vyd: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(22 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1vyd.gif|left|200px]]<br />
<applet load="1vyd" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1vyd, resolution 2.30&Aring;" />
'''CRYSTAL STRUCTURE OF CYTOCHROME C2 MUTANT G95E'''<br />


==Overview==
==Crystal structure of cytochrome C2 mutant G95E==
All class I c-type cytochromes studied to date undergo a dynamic process, in the oxidized state, which results in the transient breaking of the, iron-methionine-sulfur bond and sufficient movement to allow the binding, of exogenous ligands (imidazole in this work). In the case of Rhodobacter, capsulatus cytochrome c(2), the sixth heme ligand Met96 and up to 14, flanking residues (positions 88-100, termed the hinge region), located, between two relatively rigid helical regions, may be involved in, structural changes leading to a transient high-spin species able to bind, ligands. We have examined 14 mutations at 9 positions in the hinge region, of Rhodobacter capsulatus cytochrome c(2) and have determined the, structure of the G95E mutant. Mutations near the N- and C-terminus of the, hinge ... [[http://ispc.weizmann.ac.il/pmbin/getpm?15196014 (full description)]]
<StructureSection load='1vyd' size='340' side='right'caption='[[1vyd]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1vyd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VYD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VYD 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1vyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vyd OCA], [https://pdbe.org/1vyd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vyd RCSB], [https://www.ebi.ac.uk/pdbsum/1vyd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vyd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CYC2_RHOCB CYC2_RHOCB] 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 ==
[[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/vy/1vyd_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=1vyd ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1VYD is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]] with HEM as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VYD OCA]].
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Protein dynamics in the region of the sixth ligand methionine revealed by studies of imidazole binding to Rhodobacter capsulatus cytochrome c2 hinge mutants., Dumortier C, Fitch J, Van Petegem F, Vermeulen W, Meyer TE, Van Beeumen JJ, Cusanovich MA, Biochemistry. 2004 Jun 22;43(24):7717-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15196014 15196014]
[[Category: Large Structures]]
[[Category: Rhodobacter capsulatus]]
[[Category: Rhodobacter capsulatus]]
[[Category: Single protein]]
[[Category: Cusanovich MA]]
[[Category: Beeumen, J.J.Van.]]
[[Category: Dumortier C]]
[[Category: Cusanovich, M.A.]]
[[Category: Fitch J]]
[[Category: Dumortier, C.]]
[[Category: Meyer TE]]
[[Category: Fitch, J.]]
[[Category: Van Beeumen JJ]]
[[Category: Meyer, T.E.]]
[[Category: Van Petegem F]]
[[Category: Petegem, F.Van.]]
[[Category: Vermeulen W]]
[[Category: Vermeulen, W.]]
[[Category: HEM]]
[[Category: cytochrome c2]]
[[Category: electron transport]]
[[Category: mutant]]
[[Category: redox]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:05:30 2007''

Latest revision as of 09:36, 1 May 2024

Crystal structure of cytochrome C2 mutant G95ECrystal structure of cytochrome C2 mutant G95E

Structural highlights

1vyd is a 2 chain structure with sequence from Rhodobacter capsulatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CYC2_RHOCB 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.

See Also

1vyd, resolution 2.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1vyd&oldid=4135220"