2c1d: Difference between revisions

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[[Image:2c1d.~~gif~~|left|200px]]

[[Image:2c1d.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF SOXXA FROM P. PANTOTROPHUS~~'''~~

===CRYSTAL STRUCTURE OF SOXXA FROM P. PANTOTROPHUS===

~~==Overview==~~

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The ~~sulfur-oxidizing enzyme system (Sox) of the chemotroph Paracoccus pantotrophus is composed of several proteins~~, ~~which together oxidize hydrogen sulfide~~, ~~sulfur, thiosulfate or sulfite and transfers~~ the ~~gained electrons~~ to the ~~respiratory chain~~. ~~The hetero-dimeric cytochrome c complex SoxXA functions as heme enzyme and links covalently the sulfur substrate to the thiol of the cysteine-138 residue of the SoxY protein of the SoxYZ complex~~. ~~Here~~, ~~we report~~ the ~~crystal structure of the c-type cytochrome complex SoxXA~~. ~~The structure could be solved by molecular replacement and refined to a resolution of 1.9A identifying the axial heme~~-~~iron coordination involving an unusual Cys~~-251 thiolate of heme2. Distance measurements between the three heme groups provide deeper insight into the electron transport inside SoxXA and merge in a better understanding of the initial step of the aerobic sulfur oxidation process in chemotrophic bacteria.

The line below this paragraph, {{ABSTRACT_PUBMED_16297640}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16297640 is the PubMed ID number.

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==About this Structure==

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[[Category: Oxidoreductase]]

[[Category: Sulfur oxidation]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 21~~:05:38 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:23:07 2008''

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-[[Image:2c1d.gif|left|200px]]
+{{Seed}}
+[[Image:2c1d.png|left|200px]]
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 {{STRUCTURE_2c1d|  PDB=2c1d  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF SOXXA FROM P. PANTOTROPHUS'''
+===CRYSTAL STRUCTURE OF SOXXA FROM P. PANTOTROPHUS===
-==Overview==
+<!--
-The sulfur-oxidizing enzyme system (Sox) of the chemotroph Paracoccus pantotrophus is composed of several proteins, which together oxidize hydrogen sulfide, sulfur, thiosulfate or sulfite and transfers the gained electrons to the respiratory chain. The hetero-dimeric cytochrome c complex SoxXA functions as heme enzyme and links covalently the sulfur substrate to the thiol of the cysteine-138 residue of the SoxY protein of the SoxYZ complex. Here, we report the crystal structure of the c-type cytochrome complex SoxXA. The structure could be solved by molecular replacement and refined to a resolution of 1.9A identifying the axial heme-iron coordination involving an unusual Cys-251 thiolate of heme2. Distance measurements between the three heme groups provide deeper insight into the electron transport inside SoxXA and merge in a better understanding of the initial step of the aerobic sulfur oxidation process in chemotrophic bacteria.
+The line below this paragraph, {{ABSTRACT_PUBMED_16297640}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16297640 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16297640}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Oxidoreductase]]
 [[Category: Sulfur oxidation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 21:05:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:23:07 2008''