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2zp9

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Revision as of 02:12, 5 August 2016

The Nature of the TRAP:Anti-TRAP complex

Structural highlights

2zp9 is a 15 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900 and Atcc 12980. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2zcz, 2zp8
Gene:	mtrB (ATCC 12980), rtpA, yczA, BSU02530 ("Bacillus globigii" Migula 1900)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RTPA_BACSU] By forming a complex with tryptophan-activated TRAP, and masking its RNA binding site, it inhibits TRAP's RNA binding ability, thereby abolishing TRAP regulation of gene expression, leading to antitermination and increased trp operon expression. AT acts by competing with messenger RNA for the RNA binding domain of TRAP.

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

Tryptophan biosynthesis is subject to exquisite control in species of Bacillus and has become one of the best-studied model systems in gene regulation. The protein TRAP (trp RNA-binding attenuation protein) predominantly forms a ring-shaped 11-mer, which binds cognate RNA in the presence of tryptophan to suppress expression of the trp operon. TRAP is itself regulated by the protein Anti-TRAP, which binds to TRAP and prevents RNA binding. To date, the nature of this interaction has proved elusive. Here, we describe mass spectrometry and analytical centrifugation studies of the complex, and 2 crystal structures of the TRAP-Anti-TRAP complex. These crystal structures, both refined to 3.2-A resolution, show that Anti-TRAP binds to TRAP as a trimer, sterically blocking RNA binding. Mass spectrometry shows that 11-mer TRAP may bind up to 5 AT trimers, and an artificial 12-mer TRAP may bind 6. Both forms of TRAP make the same interactions with Anti-TRAP. Crystallization of wild-type TRAP with Anti-TRAP selectively pulls the 12-mer TRAP form out of solution, so the crystal structure of wild-type TRAP-Anti-TRAP complex reflects a minor species from a mixed population.

The nature of the TRAP-Anti-TRAP complex.,Watanabe M, Heddle JG, Kikuchi K, Unzai S, Akashi S, Park SY, Tame JR Proc Natl Acad Sci U S A. 2009 Jan 22. PMID:19164760^[1]

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

References

↑ Watanabe M, Heddle JG, Kikuchi K, Unzai S, Akashi S, Park SY, Tame JR. The nature of the TRAP-Anti-TRAP complex. Proc Natl Acad Sci U S A. 2009 Jan 22. PMID:19164760

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2zp9"

@@ Line 1: / Line 1: @@
 ==The Nature of the TRAP:Anti-TRAP complex==
 <StructureSection load='2zp9' size='340' side='right' caption='[[2zp9]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zcz|2zcz]], [[2zp8|2zp8]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mtrB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980]), rtpA, yczA, BSU02530 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</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=2zp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zp9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zp9 RCSB], [http://www.ebi.ac.uk/pdbsum/2zp9 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=2zp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zp9 OCA], [http://pdbe.org/2zp9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zp9 RCSB], [http://www.ebi.ac.uk/pdbsum/2zp9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zp9 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2zp9 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2zp9" style="background-color:#fffaf0;"></div>
 ==See Also==

2zp9

From Proteopedia

Revision as of 02:12, 5 August 2016

The Nature of the TRAP:Anti-TRAP complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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