1y9x

From Proteopedia

(Difference between revisions)

Revision as of 07:09, 25 April 2018

Solution structure of Archaeon DNA-binding protein ssh10b

Structural highlights

1y9x is a 2 chain structure with sequence from 'saccharolobus shibatae'. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	albA1, ssh10b ('Saccharolobus shibatae')
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ALBA1_SULSH] Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. May be involved in DNA compaction. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.[HAMAP-Rule:MF_01122]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The hyperthermophilic Ssh10b from Sulfolobus shibatae is a member of the Sac10b family, which has been postulated to play a role in chromosomal organization in Archaea. Ssh10b is capable of significantly constraining negative DNA supercoils at elevated temperatures. In this study, the solution structure of the dimeric P62A mutant Ssh10b ([P62A]Ssh10b) was determined by multidimensional NMR spectroscopy. The backbone 15N dynamics, H/D exchange with and without the denaturant GdmSCN, and chemical and thermal denaturation experiments were performed to investigate the molecular basis of high thermostability of [P62A]Ssh10b. Data analysis has revealed an alpha/beta-hydrophobic core consisting of two alpha-helices and one beta-sheet which are stabilized by cooperative hydrophobic and hydrogen-bonding interactions. This stabilizing alpha/beta-hydrophobic core of [P62A]Ssh10b exhibiting highly restricted internal motions is composed of residues having highly protected amide protons which exchange with solvent mostly by means of a global unfolding process. The K40N mutation greatly destabilizes the mutant [P62A]Ssh10b because this mutation disturbs the packing of alpha-helix against the beta-sheet reducing the stability of the alpha/beta-hydrophobic core in the mutant protein. In comparison with homologous mesophilic and thermophilic proteins, it can be presumed that the stabilizing alpha/beta-hydrophobic core in the [P62A]Ssh10b structure greatly contributes to the high thermostability of the protein.

A stabilizing alpha/beta-hydrophobic core greatly contributes to hyperthermostability of archaeal [P62A]Ssh10b.,Fang X, Cui Q, Tong Y, Feng Y, Shan L, Huang L, Wang J Biochemistry. 2008 Oct 28;47(43):11212-21. Epub 2008 Sep 27. PMID:18821773^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Fang X, Cui Q, Tong Y, Feng Y, Shan L, Huang L, Wang J. A stabilizing alpha/beta-hydrophobic core greatly contributes to hyperthermostability of archaeal [P62A]Ssh10b. Biochemistry. 2008 Oct 28;47(43):11212-21. Epub 2008 Sep 27. PMID:18821773 doi:10.1021/bi8007593

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1y9x"

@@ Line 1: / Line 1: @@
 ==Solution structure of Archaeon DNA-binding protein ssh10b==
 <StructureSection load='1y9x' size='340' side='right' caption='[[1y9x]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1y9x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51178 Atcc 51178]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y9X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1y9x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/'saccharolobus_shibatae' 'saccharolobus shibatae']. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y9X FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">albA1, ssh10b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2286 ATCC 51178])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">albA1, ssh10b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2286 'Saccharolobus shibatae'])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y9x OCA], [http://pdbe.org/1y9x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y9x RCSB], [http://www.ebi.ac.uk/pdbsum/1y9x PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y9x OCA], [http://pdbe.org/1y9x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y9x RCSB], [http://www.ebi.ac.uk/pdbsum/1y9x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y9x ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y9/1y9x_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y9/1y9x_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 31: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 51178]]
+[[Category: Saccharolobus shibatae]]
 [[Category: Cui, Q]]
 [[Category: Tong, Y]]

1y9x

From Proteopedia

Revision as of 07:09, 25 April 2018

Solution structure of Archaeon DNA-binding protein ssh10b

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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