1nlf: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1nlf.jpg|left|200px]]<br /><applet load="1nlf" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1nlf.jpg|left|200px]]
caption="1nlf, resolution 1.95&Aring;" />
 
'''Crystal Structure of DNA Helicase RepA in complex with sulfate at 1.95 A resolution'''<br />
{{Structure
|PDB= 1nlf |SIZE=350|CAPTION= <scene name='initialview01'>1nlf</scene>, resolution 1.95&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|ACTIVITY=
|GENE= REPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
}}
 
'''Crystal Structure of DNA Helicase RepA in complex with sulfate at 1.95 A resolution'''
 


==Overview==
==Overview==
Line 7: Line 16:


==About this Structure==
==About this Structure==
1NLF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLF OCA].  
1NLF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLF OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12777796 12777796]
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:[http://www.ncbi.nlm.nih.gov/pubmed/12777796 12777796]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 20: Line 29:
[[Category: Xu, H.]]
[[Category: Xu, H.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: replicative dna helicase structural changes]]
[[Category: replicative dna helicase structural change]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:19 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:58:24 2008''

Revision as of 13:58, 20 March 2008

File:1nlf.jpg


PDB ID 1nlf

Drag the structure with the mouse to rotate
, resolution 1.95Å
Ligands:
Gene: REPA (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of DNA Helicase RepA in complex with sulfate at 1.95 A resolution


OverviewOverview

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 StructureAbout this Structure

1NLF is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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 Thu Mar 20 12:58:24 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA