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3boy

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Revision as of 08:07, 25 October 2017

Crystal structure of the HutP antitermination complex bound to the HUT mRNA

Structural highlights

3boy is a 4 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. This structure supersedes the now removed PDB entry 2gzt. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1vea, 1wpt, 1wmq, 1wpu, 1wrq, 1wpv
Gene:	hutP ("Bacillus globigii" Migula 1900)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[HUTP_BACSU] Antiterminator that binds to cis-acting regulatory sequences on the mRNA in the presence of histidine, thereby suppressing transcription termination and activating the hut operon for histidine utilization.[HAMAP-Rule:MF_00779]

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

HutP is an L-histidine-activated RNA binding protein that regulates the expression of the histidine utilization (hut) operon in Bacillus subtilis by binding to cis-acting regulatory sequences on the hut mRNA. The crystal structure of HutP complexed with an L-histidine analog showed a novel fold; there are four antiparallel beta strands in the central region of each monomer, with two alpha helices each on the front and back. Two HutP monomers form a dimer, and three dimers are arranged in crystallographic 3-fold symmetry to form a hexamer. A histidine analog was located in between the two monomers of HutP, with the imidazole group of L-histidine hydrogen bonded to Glu81. An activation mechanism is proposed based on the identification of key residues of HutP. The HutP binding region in hut mRNA was defined: it consists of three UAG trinucleotide motifs separated by four spacer nucleotides. Residues of HutP potentially important for RNA binding were identified.

Crystal structure of activated HutP; an RNA binding protein that regulates transcription of the hut operon in Bacillus subtilis.,Kumarevel T, Fujimoto Z, Karthe P, Oda M, Mizuno H, Kumar PK Structure. 2004 Jul;12(7):1269-80. PMID:15242603^[1]

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

References

↑ Kumarevel T, Fujimoto Z, Karthe P, Oda M, Mizuno H, Kumar PK. Crystal structure of activated HutP; an RNA binding protein that regulates transcription of the hut operon in Bacillus subtilis. Structure. 2004 Jul;12(7):1269-80. PMID:15242603 doi:http://dx.doi.org/10.1016/j.str.2004.05.005

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/3boy"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the HutP antitermination complex bound to the HUT mRNA==
 <StructureSection load='3boy' size='340' side='right' caption='[[3boy]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vea|1vea]], [[1wpt|1wpt]], [[1wmq|1wmq]], [[1wpu|1wpu]], [[1wrq|1wrq]], [[1wpv|1wpv]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hutP ([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=3boy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3boy OCA], [http://pdbe.org/3boy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3boy RCSB], [http://www.ebi.ac.uk/pdbsum/3boy PDBsum], [http://www.topsan.org/Proteins/RSGI/3boy TOPSAN]</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=3boy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3boy OCA], [http://pdbe.org/3boy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3boy RCSB], [http://www.ebi.ac.uk/pdbsum/3boy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3boy ProSAT], [http://www.topsan.org/Proteins/RSGI/3boy TOPSAN]</span></td></tr>
 </table>
 == Function ==

3boy

From Proteopedia

Revision as of 08:07, 25 October 2017

Crystal structure of the HutP antitermination complex bound to the HUT mRNA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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