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1g2h

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Revision as of 00:48, 25 December 2014

SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF THE TYRR PROTEIN OF HAEMOPHILUS INFLUENZAE

Structural highlights

1g2h is a 1 chain structure with sequence from Haemophilus influenzae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[TYRR_HAEIN] Involved in transcriptional regulation of aromatic amino acid biosynthesis and transport.

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

The TyrR protein of Haemophilus influenzae is a 36-kD transcription factor whose major function is to control the expression of genes important in the biosynthesis and transport of aromatic amino acids. Using (1)H and (15)N NMR spectroscopy, we have determined the 3D solution structure of the TyrR C-terminal DNA-binding domain (DBD) containing residues from 258 to 318 (TyrR[258-318]). The NMR results show that this segment of TyrR consists of a potential hinge helix at its N terminus (residues 263-270) as well as three well-defined alpha-helices extending from residues 277-289 (HR-2), 293-300 (HR-1), and 304-314 (HR). Helix HR-1 and HR fold in a typical helix-turn-helix (HTH) motif. The three helices and the hinge helix are tightly bound together by hydrophobic interaction and hydrogen bonds. Several hydrophilic residues whose side chains may directly interact with DNA are identified. A hydrophobic patch that may be part of the interaction surface between the domains of TyrR protein is also observed. Comparisons with the structures of other HTH DNA-binding proteins reveal that in terms of the spatial orientation of the three helices, this protein most closely resembles the cap family.

Solution structure of the DNA-binding domain of the TyrR protein of Haemophilus influenzae.,Wang Y, Zhao S, Somerville RL, Jardetzky O Protein Sci. 2001 Mar;10(3):592-8. PMID:11344327^[1]

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

References

↑ Wang Y, Zhao S, Somerville RL, Jardetzky O. Solution structure of the DNA-binding domain of the TyrR protein of Haemophilus influenzae. Protein Sci. 2001 Mar;10(3):592-8. PMID:11344327

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/1g2h"

@@ Line 5: / Line 5: @@
 </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=1g2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g2h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g2h RCSB], [http://www.ebi.ac.uk/pdbsum/1g2h PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/TYRR_HAEIN TYRR_HAEIN]] Involved in transcriptional regulation of aromatic amino acid biosynthesis and transport.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1g2h

From Proteopedia

Revision as of 00:48, 25 December 2014

SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF THE TYRR PROTEIN OF HAEMOPHILUS INFLUENZAE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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