1a5t: Difference between revisions

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[[Image:1a5t.~~gif~~|left|200px]]

[[Image:1a5t.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF THE DELTA PRIME SUBUNIT OF THE CLAMP-LOADER COMPLEX OF ESCHERICHIA COLI DNA POLYMERASE III~~'''~~

===CRYSTAL STRUCTURE OF THE DELTA PRIME SUBUNIT OF THE CLAMP-LOADER COMPLEX OF ESCHERICHIA COLI DNA POLYMERASE III===

~~==Overview==~~

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The ~~crystal structure of~~ the ~~delta' subunit of~~ the ~~clamp-loader complex of E~~. ~~coli DNA polymerase III has been determined~~. Three consecutive domains in the structure are arranged in a C-shaped architecture. The N-terminal domain contains a nonfunctional nucleotide binding site. The catalytic component of the clamp-loader complex is the gamma subunit, ~~which~~ is ~~homologous to delta'. A sequence-structure alignment suggests that nucleotides bind to gamma at an interdomain interface within the inner surface of~~ the "C.~~" The alignment is extended to other clamp~~-~~loader complexes and to the RuvB family of DNA helicases, and suggests that each of these is assembled from C~~-~~shaped components that can open and close the jaws of the "C" in response to ATP binding and hydrolysis.~~

The line below this paragraph, {{ABSTRACT_PUBMED_9363942}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9363942 is the PubMed ID number.

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==About this Structure==

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[[Category: Dna replication]]

[[Category: Zinc finger]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 09~~:51:15 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:11:53 2008''

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-[[Image:1a5t.gif|left|200px]]
+{{Seed}}
+[[Image:1a5t.png|left|200px]]
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 {{STRUCTURE_1a5t|  PDB=1a5t  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE DELTA PRIME SUBUNIT OF THE CLAMP-LOADER COMPLEX OF ESCHERICHIA COLI DNA POLYMERASE III'''
+===CRYSTAL STRUCTURE OF THE DELTA PRIME SUBUNIT OF THE CLAMP-LOADER COMPLEX OF ESCHERICHIA COLI DNA POLYMERASE III===
-==Overview==
+<!--
-The crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III has been determined. Three consecutive domains in the structure are arranged in a C-shaped architecture. The N-terminal domain contains a nonfunctional nucleotide binding site. The catalytic component of the clamp-loader complex is the gamma subunit, which is homologous to delta'. A sequence-structure alignment suggests that nucleotides bind to gamma at an interdomain interface within the inner surface of the "C." The alignment is extended to other clamp-loader complexes and to the RuvB family of DNA helicases, and suggests that each of these is assembled from C-shaped components that can open and close the jaws of the "C" in response to ATP binding and hydrolysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_9363942}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9363942 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9363942}}
 ==About this Structure==
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 [[Category: Dna replication]]
 [[Category: Zinc finger]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:51:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:11:53 2008''