3afq: Difference between revisions

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[[Image:3afq.jpg|left|200px]]


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==Crystal structure of the single-stranded DNA binding protein from Mycobacterium leprae (Form II)==
The line below this paragraph, containing "STRUCTURE_3afq", creates the "Structure Box" on the page.
<StructureSection load='3afq' size='340' side='right'caption='[[3afq]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3afq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_leprae_TN Mycobacterium leprae TN]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AFQ FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-->
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3afq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3afq OCA], [https://pdbe.org/3afq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3afq RCSB], [https://www.ebi.ac.uk/pdbsum/3afq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3afq ProSAT]</span></td></tr>
{{STRUCTURE_3afq|  PDB=3afq  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/SSB_MYCLE SSB_MYCLE]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/af/3afq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3afq ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structures of two forms of Mycobacterium leprae single-stranded DNA-binding protein (SSB) have been determined at 2.05 and 2.8 A resolution. Comparison of these structures with the structures of other eubacterial SSBs indicates considerable variation in their quaternary association, although the DNA-binding domains in all of them exhibit the same OB-fold. This variation has no linear correlation with sequence variation, but could be related to variation in protein stability. Molecular-dynamics simulations have been carried out on tetrameric molecules derived from the two forms and the prototype Escherichia coli SSB and the individual subunits of both proteins. Together, the X-ray studies and molecular-dynamics simulations yield information on the relatively rigid and flexible regions of the molecule and on the effect of oligomerization on flexibility. The simulations provide insight into the changes in subunit structure on oligomerization. They also provide insight into the stability and time evolution of the hydrogen bonds/water bridges that connect the two pairs of monomers in the tetramer.


===Crystal structure of the single-stranded DNA binding protein from Mycobacterium leprae (Form II)===
X-ray and molecular-dynamics studies on Mycobacterium leprae single-stranded DNA-binding protein and comparison with other eubacterial SSB structures.,Kaushal PS, Singh P, Sharma A, Muniyappa K, Vijayan M Acta Crystallogr D Biol Crystallogr. 2010 Oct;66(Pt 10):1048-58. Epub 2010 Sep, 18. PMID:20944238<ref>PMID:20944238</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3afq" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
3AFQ is a 4 chains structure with sequences from [http://en.wikipedia.org/wiki/Mycobacterium_leprae Mycobacterium leprae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AFQ OCA].
*[[Single-stranded DNA-binding protein 3D structures|Single-stranded DNA-binding protein 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:16041080</ref><ref group="xtra">PMID:12888346</ref><ref group="xtra">PMID:9033597</ref><ref group="xtra">PMID:9192620</ref><references group="xtra"/>
__TOC__
[[Category: Mycobacterium leprae]]
</StructureSection>
[[Category: Kaushal, P S.]]
[[Category: Large Structures]]
[[Category: Muniyappa, K.]]
[[Category: Mycobacterium leprae TN]]
[[Category: Sharma, A.]]
[[Category: Kaushal PS]]
[[Category: Singh, P.]]
[[Category: Muniyappa K]]
[[Category: Vijayan, M.]]
[[Category: Sharma A]]
[[Category: Changes on oligomerisation]]
[[Category: Singh P]]
[[Category: Dna binding protein]]
[[Category: Vijayan M]]
[[Category: Dna damage]]
[[Category: Dna repair]]
[[Category: Dna replication]]
[[Category: Dna-binding]]
[[Category: Ob-fold]]
[[Category: Quaternary structure and stability]]
[[Category: Water-bridge]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct  6 06:03:50 2010''

Latest revision as of 17:24, 1 November 2023

Crystal structure of the single-stranded DNA binding protein from Mycobacterium leprae (Form II)Crystal structure of the single-stranded DNA binding protein from Mycobacterium leprae (Form II)

Structural highlights

3afq is a 4 chain structure with sequence from Mycobacterium leprae TN. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SSB_MYCLE

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 crystal structures of two forms of Mycobacterium leprae single-stranded DNA-binding protein (SSB) have been determined at 2.05 and 2.8 A resolution. Comparison of these structures with the structures of other eubacterial SSBs indicates considerable variation in their quaternary association, although the DNA-binding domains in all of them exhibit the same OB-fold. This variation has no linear correlation with sequence variation, but could be related to variation in protein stability. Molecular-dynamics simulations have been carried out on tetrameric molecules derived from the two forms and the prototype Escherichia coli SSB and the individual subunits of both proteins. Together, the X-ray studies and molecular-dynamics simulations yield information on the relatively rigid and flexible regions of the molecule and on the effect of oligomerization on flexibility. The simulations provide insight into the changes in subunit structure on oligomerization. They also provide insight into the stability and time evolution of the hydrogen bonds/water bridges that connect the two pairs of monomers in the tetramer.

X-ray and molecular-dynamics studies on Mycobacterium leprae single-stranded DNA-binding protein and comparison with other eubacterial SSB structures.,Kaushal PS, Singh P, Sharma A, Muniyappa K, Vijayan M Acta Crystallogr D Biol Crystallogr. 2010 Oct;66(Pt 10):1048-58. Epub 2010 Sep, 18. PMID:20944238[1]

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

See Also

References

  1. Kaushal PS, Singh P, Sharma A, Muniyappa K, Vijayan M. X-ray and molecular-dynamics studies on Mycobacterium leprae single-stranded DNA-binding protein and comparison with other eubacterial SSB structures. Acta Crystallogr D Biol Crystallogr. 2010 Oct;66(Pt 10):1048-58. Epub 2010 Sep, 18. PMID:20944238 doi:10.1107/S0907444910032208

3afq, resolution 2.80Å

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