1qn2: Difference between revisions

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{{Seed}}
[[Image:1qn2.png|left|200px]]


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==cytochrome cH from Methylobacterium extorquens==
The line below this paragraph, containing "STRUCTURE_1qn2", creates the "Structure Box" on the page.
<StructureSection load='1qn2' size='340' side='right'caption='[[1qn2]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1qn2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylorubrum_extorquens Methylorubrum extorquens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QN2 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</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>
{{STRUCTURE_1qn2|  PDB=1qn2  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qn2 OCA], [https://pdbe.org/1qn2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qn2 RCSB], [https://www.ebi.ac.uk/pdbsum/1qn2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qn2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q7SIA4_METEX Q7SIA4_METEX]
== 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/qn/1qn2_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=1qn2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytochrome cH is the electron donor to the oxidase in methylotrophic bacteria. Its amino acid sequence suggests that it is a typical Class 1 cytochrome c, but some features of the sequence indicated that its structure might be of special interest. The structure of oxidized cytochrome cH has been solved to 2.0 A resolution by X-ray diffraction. It has the classical tertiary structure of the Class 1 cytochromes c but bears a closer gross resemblance to mitochondrial cytochrome c than to the bacterial cytochrome c2. The left-hand side of the haem cleft is unique; in particular, it is highly hydrophobic, the usual water is absent, and the "conserved" Tyr67 is replaced by tryptophan. A number of features of the structure demonstrate that the usual hydrogen bonding network involving water in the haem channel is not essential and that other mechanisms may exist for modulation of redox potentials in this cytochrome.


===CYTOCHROME CH FROM METHYLOBACTERIUM EXTORQUENS===
The molecular structure of an unusual cytochrome c2 determined at 2.0 A; the cytochrome cH from Methylobacterium extorquens.,Read J, Gill R, Dales SL, Cooper JB, Wood SP, Anthony C Protein Sci. 1999 Jun;8(6):1232-40. PMID:10386873<ref>PMID:10386873</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1qn2" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_10386873}}, adds the Publication Abstract to the page
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 10386873 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_10386873}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1QN2 is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Methylobacterium_extorquens Methylobacterium extorquens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QN2 OCA].
[[Category: Methylorubrum extorquens]]
 
[[Category: Anthony C]]
==Reference==
[[Category: Cooper JB]]
<ref group="xtra">PMID:10386873</ref><references group="xtra"/>
[[Category: Dales SL]]
[[Category: Methylobacterium extorquens]]
[[Category: Gill R]]
[[Category: Anthony, C.]]
[[Category: Read J]]
[[Category: Cooper, J B.]]
[[Category: Wood SP]]
[[Category: Dales, S L.]]
[[Category: Gill, R.]]
[[Category: Read, J.]]
[[Category: Wood, S P.]]
[[Category: Cytochrome c]]
[[Category: Electron transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 05:25:27 2009''

Latest revision as of 15:49, 13 December 2023

cytochrome cH from Methylobacterium extorquenscytochrome cH from Methylobacterium extorquens

Structural highlights

1qn2 is a 3 chain structure with sequence from Methylorubrum extorquens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.01Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q7SIA4_METEX

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

Cytochrome cH is the electron donor to the oxidase in methylotrophic bacteria. Its amino acid sequence suggests that it is a typical Class 1 cytochrome c, but some features of the sequence indicated that its structure might be of special interest. The structure of oxidized cytochrome cH has been solved to 2.0 A resolution by X-ray diffraction. It has the classical tertiary structure of the Class 1 cytochromes c but bears a closer gross resemblance to mitochondrial cytochrome c than to the bacterial cytochrome c2. The left-hand side of the haem cleft is unique; in particular, it is highly hydrophobic, the usual water is absent, and the "conserved" Tyr67 is replaced by tryptophan. A number of features of the structure demonstrate that the usual hydrogen bonding network involving water in the haem channel is not essential and that other mechanisms may exist for modulation of redox potentials in this cytochrome.

The molecular structure of an unusual cytochrome c2 determined at 2.0 A; the cytochrome cH from Methylobacterium extorquens.,Read J, Gill R, Dales SL, Cooper JB, Wood SP, Anthony C Protein Sci. 1999 Jun;8(6):1232-40. PMID:10386873[1]

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

See Also

References

  1. ↑ Read J, Gill R, Dales SL, Cooper JB, Wood SP, Anthony C. The molecular structure of an unusual cytochrome c2 determined at 2.0 A; the cytochrome cH from Methylobacterium extorquens. Protein Sci. 1999 Jun;8(6):1232-40. PMID:10386873

1qn2, resolution 2.01Å

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