1sru: Difference between revisions

Revision as of 16:04, 21 February 2008

Crystal structure of full length E. coli SSB protein

OverviewOverview

The crystal structure of full-length homotetrameric single-stranded DNA (ssDNA)-binding protein from Escherichia coli (SSB) has been determined to 3.3 A resolution and reveals that the entire C-terminal domain is disordered even in the presence of ssDNA. To our knowledge, this is the first experimental evidence that the C-terminal domain of SSB may be inherently disordered. The N-terminal DNA-binding domain of the protein is well ordered and is virtually indistinguishable from the previously determined structure of the chymotryptic fragment of SSB (SSBc) in complex with ssDNA. The absence of observable interactions with the core protein and the crystal packing of SSB together suggest that the disordered C-terminal domains likely extend laterally away from the DNA- binding domains, which may facilitate interactions with components of the replication machinery in vivo. The structure also reveals the conservation of molecular contacts between successive tetramers mediated by the L(45) loops as seen in two other crystal forms of SSBc, suggesting a possible functional relevance of this interaction.

About this StructureAbout this Structure

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

ReferenceReference

The C-terminal domain of full-length E. coli SSB is disordered even when bound to DNA., Savvides SN, Raghunathan S, Futterer K, Kozlov AG, Lohman TM, Waksman G, Protein Sci. 2004 Jul;13(7):1942-7. Epub 2004 May 28. PMID:15169953

Page seeded by OCA on Thu Feb 21 15:04:34 2008

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

OCA

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-[[Image:1sru.gif|left|200px]]<br /><applet load="1sru" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1sru.gif|left|200px]]<br /><applet load="1sru" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1sru, resolution 3.30&Aring;" />
 '''Crystal structure of full length E. coli SSB protein'''<br />
 ==Overview==
-The crystal structure of full-length homotetrameric single-stranded DNA, (ssDNA)-binding protein from Escherichia coli (SSB) has been determined to, 3.3 A resolution and reveals that the entire C-terminal domain is, disordered even in the presence of ssDNA. To our knowledge, this is the, first experimental evidence that the C-terminal domain of SSB may be, inherently disordered. The N-terminal DNA-binding domain of the protein is, well ordered and is virtually indistinguishable from the previously, determined structure of the chymotryptic fragment of SSB (SSBc) in complex, with ssDNA. The absence of observable interactions with the core protein, and the crystal packing of SSB together suggest that the disordered, C-terminal domains likely extend laterally away from the DNA- binding, domains, which may facilitate interactions with components of the, replication machinery in vivo. The structure also reveals the conservation, of molecular contacts between successive tetramers mediated by the L(45), loops as seen in two other crystal forms of SSBc, suggesting a possible, functional relevance of this interaction.
+The crystal structure of full-length homotetrameric single-stranded DNA (ssDNA)-binding protein from Escherichia coli (SSB) has been determined to 3.3 A resolution and reveals that the entire C-terminal domain is disordered even in the presence of ssDNA. To our knowledge, this is the first experimental evidence that the C-terminal domain of SSB may be inherently disordered. The N-terminal DNA-binding domain of the protein is well ordered and is virtually indistinguishable from the previously determined structure of the chymotryptic fragment of SSB (SSBc) in complex with ssDNA. The absence of observable interactions with the core protein and the crystal packing of SSB together suggest that the disordered C-terminal domains likely extend laterally away from the DNA- binding domains, which may facilitate interactions with components of the replication machinery in vivo. The structure also reveals the conservation of molecular contacts between successive tetramers mediated by the L(45) loops as seen in two other crystal forms of SSBc, suggesting a possible functional relevance of this interaction.
 ==About this Structure==
-SRU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SRU OCA].
+SRU is a [http://en.wikipedia.org/wiki/Single_protein 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=1SRU OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Fuetterer, K.]]
-[[Category: Kozlov, A.G.]]
+[[Category: Kozlov, A G.]]
-[[Category: Lohman, T.M.]]
+[[Category: Lohman, T M.]]
 [[Category: Raghunathan, S.]]
-[[Category: Savvides, S.N.]]
+[[Category: Savvides, S N.]]
 [[Category: Waksman, G.]]
 [[Category: replication]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:36:49 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:34 2008''