2ph0: Difference between revisions

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~~'''~~Crystal structure of the Q6D2T7_ERWCT protein from Erwinia carotovora. NESG target EwR41.~~'''~~

===Crystal structure of the Q6D2T7_ERWCT protein from Erwinia carotovora. NESG target EwR41.===

~~==Overview==~~

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~~We report here the crystal structure at 2.0 A resolution of the AGR_C_4470p protein from the Gram-negative bacterium Agrobacterium tumefaciens.~~ The ~~protein is a tightly associated dimer~~, ~~each subunit of which bears strong structural homology with the two domains of the heme utilization protein ChuS from Escherichia coli and HemS from Yersinia enterocolitica. Remarkably~~, the ~~organization of~~ the ~~AGR_C_4470p dimer is the same~~ as that of the two domains in ChuS and HemS, providing structural evidence that these two proteins evolved by gene duplication. However, the binding site for heme, while conserved in HemS and ChuS, is not conserved in AGR_C_4470p, suggesting that it ~~probably has a different function~~. ~~This is supported by the presence of two homologs of AGR_C_4470p in E~~. ~~coli~~, ~~in addition to~~ the ~~ChuS protein~~.

The line below this paragraph, {{ABSTRACT_PUBMED_17322535}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17322535 is the PubMed ID number.

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==About this Structure==

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[[Category: Structural genomic]]

[[Category: Unknown function]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 13~~:05:22 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Sep 29 05:39:00 2008''

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-[[Image:2ph0.gif|left|200px]]
+{{Seed}}
+[[Image:2ph0.png|left|200px]]
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 {{STRUCTURE_2ph0|  PDB=2ph0  |  SCENE=  }}
-'''Crystal structure of the Q6D2T7_ERWCT protein from Erwinia carotovora. NESG target EwR41.'''
+===Crystal structure of the Q6D2T7_ERWCT protein from Erwinia carotovora. NESG target EwR41.===
-==Overview==
+<!--
-We report here the crystal structure at 2.0 A resolution of the AGR_C_4470p protein from the Gram-negative bacterium Agrobacterium tumefaciens. The protein is a tightly associated dimer, each subunit of which bears strong structural homology with the two domains of the heme utilization protein ChuS from Escherichia coli and HemS from Yersinia enterocolitica. Remarkably, the organization of the AGR_C_4470p dimer is the same as that of the two domains in ChuS and HemS, providing structural evidence that these two proteins evolved by gene duplication. However, the binding site for heme, while conserved in HemS and ChuS, is not conserved in AGR_C_4470p, suggesting that it probably has a different function. This is supported by the presence of two homologs of AGR_C_4470p in E. coli, in addition to the ChuS protein.
+The line below this paragraph, {{ABSTRACT_PUBMED_17322535}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17322535 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17322535}}
 ==About this Structure==
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 [[Category: Structural genomic]]
 [[Category: Unknown function]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 13:05:22 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Sep 29 05:39:00 2008''