1nlf
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1nlf.jpg|left|200px]] | [[Image:1nlf.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1nlf", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1nlf| PDB=1nlf | SCENE= }} | |
| - | | | + | |
| - | | | + | |
| - | }} | + | |
'''Crystal Structure of DNA Helicase RepA in complex with sulfate at 1.95 A resolution''' | '''Crystal Structure of DNA Helicase RepA in complex with sulfate at 1.95 A resolution''' | ||
| Line 31: | Line 28: | ||
[[Category: Strater, N.]] | [[Category: Strater, N.]] | ||
[[Category: Xu, H.]] | [[Category: Xu, H.]] | ||
| - | [[Category: | + | [[Category: Replicative dna helicase structural change]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:40:24 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:40, 2 May 2008
Crystal Structure of DNA Helicase RepA in complex with sulfate at 1.95 A resolution
Overview
The structure of a new crystal form (space group C2), grown at pH 8.0 and diffracting to 1.95 A resolution, of the replicative homo-hexameric DNA helicase RepA encoded by plasmid RSF1010 is reported. In contrast to previous crystals grown at pH 6.0 in space group P2(1) (Niedenzu et al., 2001), only one half (a trimer) of the RepA hexamer occupies the asymmetric unit of the space-group C2 crystals. The new crystal packing explains the pH-dependent hexamer-hexamer association mechanism of RepA. The C-terminus (264)VLERQRKSKGVPRGEA(279), which could not be modelled in the previous structure, is clearly defined in the present electron density except for the last four amino acids. Sulfate anions occupy the six ATPase active sites of RepA at positions where the product phosphates are supposed to bind. Binding of sulfate anions induces conformational changes both at the ATPase active sites and throughout the whole molecular structure. In agreement with electron microscopy, the above studies implicate structural changes to an "open" form that may occur upon binding and hydrolysis of nucleotide 5'-triphosphates and could be essential for DNA duplex-unwinding activity.
About this Structure
1NLF is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of DNA helicase RepA in complex with sulfate at 1.95 A resolution implicates structural changes to an "open" form., Xu H, Strater N, Schroder W, Bottcher C, Ludwig K, Saenger W, Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):815-22. Epub 2003, Apr 25. PMID:12777796 Page seeded by OCA on Sat May 3 02:40:24 2008
