1gd7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1gd7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gd7, resolution 2.0&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
Current revision (23:30, 27 December 2023) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1gd7.jpg|left|200px]]<br /><applet load="1gd7" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1gd7, resolution 2.0&Aring;" />
 
-
'''CRYSTAL STRUCTURE OF A BIFUNCTIONAL PROTEIN (CSAA) WITH EXPORT-RELATED CHAPERONE AND TRNA-BINDING ACTIVITIES.'''<br />
 
-
==Overview==
+
==CRYSTAL STRUCTURE OF A BIFUNCTIONAL PROTEIN (CSAA) WITH EXPORT-RELATED CHAPERONE AND TRNA-BINDING ACTIVITIES.==
-
The CsaA protein was first characterized in Bacillus subtilis as a, molecular chaperone with export-related activities. Here we report the 2.0, Angstrom-resolution crystal structure of the Thermus thermophilus CsaA, protein, designated ttCsaA. Atomic structure and experiments in solution, revealed a homodimer as the functional unit. The structure of the ttCsaA, monomer is reminiscent of the well known oligonucleotide-binding fold, with the addition of extensions at the N- and C-termini that form an, extensive dimer interface. The two identical, large, hydrophobic cavities, on the protein surface are likely to constitute the substrate binding, sites. The CsaA proteins share essential sequence similarity with the, tRNA-binding protein Trbp111. Structure-based sequence analysis suggests a, close structural resemblance between these proteins, which may extend to, the architecture of the binding sites at the atomic level. These results, raise the intriguing possibility that CsaA proteins possess a second, tRNA-binding activity in addition to their export-related function.
+
<StructureSection load='1gd7' size='340' side='right'caption='[[1gd7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1gd7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GD7 FirstGlance]. <br>
 +
</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&#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=1gd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gd7 OCA], [https://pdbe.org/1gd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gd7 RCSB], [https://www.ebi.ac.uk/pdbsum/1gd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gd7 ProSAT], [https://www.topsan.org/Proteins/RSGI/1gd7 TOPSAN]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q9AQH8_THETH Q9AQH8_THETH]
 +
== 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/gd/1gd7_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=1gd7 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The CsaA protein was first characterized in Bacillus subtilis as a molecular chaperone with export-related activities. Here we report the 2.0 Angstrom-resolution crystal structure of the Thermus thermophilus CsaA protein, designated ttCsaA. Atomic structure and experiments in solution revealed a homodimer as the functional unit. The structure of the ttCsaA monomer is reminiscent of the well known oligonucleotide-binding fold, with the addition of extensions at the N- and C-termini that form an extensive dimer interface. The two identical, large, hydrophobic cavities on the protein surface are likely to constitute the substrate binding sites. The CsaA proteins share essential sequence similarity with the tRNA-binding protein Trbp111. Structure-based sequence analysis suggests a close structural resemblance between these proteins, which may extend to the architecture of the binding sites at the atomic level. These results raise the intriguing possibility that CsaA proteins possess a second, tRNA-binding activity in addition to their export-related function.
-
==About this Structure==
+
The crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus.,Kawaguchi S, Muller J, Linde D, Kuramitsu S, Shibata T, Inoue Y, Vassylyev DG, Yokoyama S EMBO J. 2001 Feb 1;20(3):562-9. PMID:11157762<ref>PMID:11157762</ref>
-
1GD7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GD7 OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
The crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus., Kawaguchi S, Muller J, Linde D, Kuramitsu S, Shibata T, Inoue Y, Vassylyev DG, Yokoyama S, EMBO J. 2001 Feb 1;20(3):562-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11157762 11157762]
+
</div>
-
[[Category: Single protein]]
+
<div class="pdbe-citations 1gd7" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
-
[[Category: Inoue, Y.]]
+
[[Category: Inoue Y]]
-
[[Category: Kawaguchi, S.]]
+
[[Category: Kawaguchi S]]
-
[[Category: Kuramitsu, S.]]
+
[[Category: Kuramitsu S]]
-
[[Category: Linde, D.]]
+
[[Category: Linde D]]
-
[[Category: Muller, J.]]
+
[[Category: Muller J]]
-
[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+
[[Category: Shibata T]]
-
[[Category: Shibata, T.]]
+
[[Category: Vassylyev DG]]
-
[[Category: Vassylyev, D.G.]]
+
[[Category: Yokoyama S]]
-
[[Category: Yokoyama, S.]]
+
-
[[Category: functional dimer]]
+
-
[[Category: hydrophobic cavity]]
+
-
[[Category: oligonucleotide-binding fold]]
+
-
[[Category: riken structural genomics/proteomics initiative]]
+
-
[[Category: rsgi]]
+
-
[[Category: structural genomics]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:11:50 2007''
+

Current revision

CRYSTAL STRUCTURE OF A BIFUNCTIONAL PROTEIN (CSAA) WITH EXPORT-RELATED CHAPERONE AND TRNA-BINDING ACTIVITIES.

PDB ID 1gd7

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gd7"
Personal tools