1wrq

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{{STRUCTURE_1wrq| PDB=1wrq | SCENE= }}
{{STRUCTURE_1wrq| PDB=1wrq | SCENE= }}
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'''Crystal Structure of HutP-Antitermination complex'''
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===Crystal Structure of HutP-Antitermination complex===
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==Overview==
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HutP regulates the expression of the hut structural genes of Bacillus subtilis by an anti-termination mechanism and requires two components, Mg2+ ions and L-histidine. HutP recognizes three UAG triplet units, separated by four non-conserved nucleotides on the terminator region. Here we report the 1.60-A resolution crystal structure of the quaternary complex (HutP-L-histidine-Mg2+-21-base single-stranded RNA). In the complex, the RNA adopts a novel triangular fold on the hexameric surface of HutP, without any base-pairing, and binds to the protein mostly by specific protein-base interactions. The structure explains how the HutP and RNA interactions are regulated critically by the l-histidine and Mg2+ ion through the structural rearrangement. To gain insights into these structural rearrangements, we solved two additional crystal structures (uncomplexed HutP and HutP-L-histidine-Mg2+) that revealed the intermediate structures of HutP (before forming an active structure) and the importance of the Mg2+ ion interactions in the complexes.
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{{ABSTRACT_PUBMED_15758992}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structural basis of HutP-mediated anti-termination and roles of the Mg2+ ion and L-histidine ligand., Kumarevel T, Mizuno H, Kumar PK, Nature. 2005 Mar 10;434(7030):183-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15758992 15758992]
Structural basis of HutP-mediated anti-termination and roles of the Mg2+ ion and L-histidine ligand., Kumarevel T, Mizuno H, Kumar PK, Nature. 2005 Mar 10;434(7030):183-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15758992 15758992]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15242603 15242603]
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Identification of important chemical groups of the hut mRNA for HutP interactions that regulate the hut operon in Bacillus subtilis., Kumarevel TS, Gopinath SC, Nishikawa S, Mizuno H, Kumar PK, Nucleic Acids Res. 2004 Jul 25;32(13):3904-12. Print 2004. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15273277 15273277]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Metal ion]]
[[Category: Metal ion]]
[[Category: Rna binding protein]]
[[Category: Rna binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:03:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:54:08 2008''

Revision as of 20:54, 28 July 2008

Image:1wrq.png

Template:STRUCTURE 1wrq

Crystal Structure of HutP-Antitermination complex

Template:ABSTRACT PUBMED 15758992

About this Structure

1WRQ is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Structural basis of HutP-mediated anti-termination and roles of the Mg2+ ion and L-histidine ligand., Kumarevel T, Mizuno H, Kumar PK, Nature. 2005 Mar 10;434(7030):183-91. PMID:15758992

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

Identification of important chemical groups of the hut mRNA for HutP interactions that regulate the hut operon in Bacillus subtilis., Kumarevel TS, Gopinath SC, Nishikawa S, Mizuno H, Kumar PK, Nucleic Acids Res. 2004 Jul 25;32(13):3904-12. Print 2004. PMID:15273277

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