1key: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(14 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1key.gif|left|200px]]<br /><applet load="1key" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1key, resolution 2.65&Aring;" />
'''Crystal Structure of Mouse Testis/Brain RNA-binding Protein (TB-RBP)'''<br />


==Overview==
==Crystal Structure of Mouse Testis/Brain RNA-binding Protein (TB-RBP)==
The testis/brain-RNA-binding protein (TB-RBP) spatially and temporally controls the expression of specific mRNAs in developing male germ cells and brain cells, and is implicated in DNA recombination and repair events. We report the 2.65 A crystal structure of mouse TB-RBP. The structure is predominantly alpha-helical and exhibits a novel protein fold and mode of assembly. Crystal symmetry and molecular symmetry combine to form an octet of TB-RBP monomers in the shape of an elongated spherical particle with a large cavity at its center. Amino acid residues that affect RNA and DNA binding are located on the interior surface of the assembled particle, and a putative nucleotide-binding domain that controls RNA binding is located at a dimer interface. Other modes of assembly are suggested for TB-RBP based on our structure and recently reported electron microscopic reconstructions of human TB-RBP.
<StructureSection load='1key' size='340' side='right'caption='[[1key]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1key]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KEY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KEY FirstGlance]. <br>
1KEY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KEY OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#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=1key FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1key OCA], [https://pdbe.org/1key PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1key RCSB], [https://www.ebi.ac.uk/pdbsum/1key PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1key ProSAT]</span></td></tr>
==Reference==
</table>
Crystal structure of TB-RBP, a novel RNA-binding and regulating protein., Pascal JM, Hart PJ, Hecht NB, Robertus JD, J Mol Biol. 2002 Jun 21;319(5):1049-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12079346 12079346]
== Function ==
[https://www.uniprot.org/uniprot/TSN_MOUSE TSN_MOUSE] DNA-binding protein that specifically recognizes consensus sequences at the breakpoint junctions in chromosomal translocations, mostly involving immunoglobulin (Ig)/T-cell receptor gene segments. Seems to recognize single-stranded DNA ends generated by staggered breaks occurring at recombination hot spots.<ref>PMID:15491149</ref>  Exhibits both single-stranded and double-stranded endoribonuclease activity. May act as an activator of RNA-induced silencing complex (RISC) by facilitating endonucleolytic cleavage of the siRNA passenger strand.<ref>PMID:15491149</ref>
== 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/ke/1key_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=1key ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Hart PJ]]
[[Category: Hart, P J.]]
[[Category: Hecht NB]]
[[Category: Hecht, N B.]]
[[Category: Pascal JM]]
[[Category: Pascal, J M.]]
[[Category: Robertus JD]]
[[Category: Robertus, J D.]]
[[Category: apotb-rbp]]
[[Category: rna-binding protein]]
[[Category: tetramer/octamer assembly]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:23 2008''

Latest revision as of 10:46, 7 February 2024

Crystal Structure of Mouse Testis/Brain RNA-binding Protein (TB-RBP)Crystal Structure of Mouse Testis/Brain RNA-binding Protein (TB-RBP)

Structural highlights

1key is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.65Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TSN_MOUSE DNA-binding protein that specifically recognizes consensus sequences at the breakpoint junctions in chromosomal translocations, mostly involving immunoglobulin (Ig)/T-cell receptor gene segments. Seems to recognize single-stranded DNA ends generated by staggered breaks occurring at recombination hot spots.[1] Exhibits both single-stranded and double-stranded endoribonuclease activity. May act as an activator of RNA-induced silencing complex (RISC) by facilitating endonucleolytic cleavage of the siRNA passenger strand.[2]

Evolutionary Conservation

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

References

  1. ↑ Wang J, Boja ES, Oubrahim H, Chock PB. Testis brain ribonucleic acid-binding protein/translin possesses both single-stranded and double-stranded ribonuclease activities. Biochemistry. 2004 Oct 26;43(42):13424-31. PMID:15491149 doi:http://dx.doi.org/10.1021/bi048847l
  2. ↑ Wang J, Boja ES, Oubrahim H, Chock PB. Testis brain ribonucleic acid-binding protein/translin possesses both single-stranded and double-stranded ribonuclease activities. Biochemistry. 2004 Oct 26;43(42):13424-31. PMID:15491149 doi:http://dx.doi.org/10.1021/bi048847l

1key, resolution 2.65Å

Drag the structure with the mouse to rotate

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

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1key&oldid=4045815"