1gu2: Difference between revisions

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[[Image:1gu2.~~jpg~~|left|200px]]

[[Image:1gu2.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF OXIDIZED CYTOCHROME C" FROM METHYLOPHILUS METHYLOTROPHUS~~'''~~

===CRYSTAL STRUCTURE OF OXIDIZED CYTOCHROME C" FROM METHYLOPHILUS METHYLOTROPHUS===

~~==Overview==~~

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The crystal structures of the oxidized and reduced forms of cytochrome c" from Methylophilus methylotrophus were solved from X-ray synchrotron data to atomic resolution. The overall fold of the molecule in the two redox states is very similar and is comparable to that of the oxygen-binding protein from the purple phototrophic bacterium Rhodobacter sphaeroides. However, ~~significant modifications occur near the haem group~~, ~~in particular~~ the ~~detachment from axial binding of His95 observed upon reduction as well as the adoption of different conformations of some protonatable residues that form a possible proton path from the haem pocket~~ to the ~~protein surface~~. ~~These changes are associated with the previously well characterized redox-Bohr behaviour of this protein~~. ~~Furthermore they provide a model for one of the presently proposed mechanisms of proton translocation in~~ the ~~much more complex protein cytochrome c oxidase~~.

The line below this paragraph, {{ABSTRACT_PUBMED_16341897}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16341897 is the PubMed ID number.

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==About this Structure==

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[[Category: Electron transport]]

[[Category: Oxidoreductase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 18~~:00:26 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:04:48 2008''

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-[[Image:1gu2.jpg|left|200px]]
+{{Seed}}
+[[Image:1gu2.png|left|200px]]
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 {{STRUCTURE_1gu2|  PDB=1gu2  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF OXIDIZED CYTOCHROME C" FROM METHYLOPHILUS METHYLOTROPHUS'''
+===CRYSTAL STRUCTURE OF OXIDIZED CYTOCHROME C" FROM METHYLOPHILUS METHYLOTROPHUS===
-==Overview==
+<!--
-The crystal structures of the oxidized and reduced forms of cytochrome c" from Methylophilus methylotrophus were solved from X-ray synchrotron data to atomic resolution. The overall fold of the molecule in the two redox states is very similar and is comparable to that of the oxygen-binding protein from the purple phototrophic bacterium Rhodobacter sphaeroides. However, significant modifications occur near the haem group, in particular the detachment from axial binding of His95 observed upon reduction as well as the adoption of different conformations of some protonatable residues that form a possible proton path from the haem pocket to the protein surface. These changes are associated with the previously well characterized redox-Bohr behaviour of this protein. Furthermore they provide a model for one of the presently proposed mechanisms of proton translocation in the much more complex protein cytochrome c oxidase.
+The line below this paragraph, {{ABSTRACT_PUBMED_16341897}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16341897 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16341897}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Electron transport]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:00:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 06:04:48 2008''