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1k1c

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{{STRUCTURE_1k1c| PDB=1k1c | SCENE= }}
{{STRUCTURE_1k1c| PDB=1k1c | SCENE= }}
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'''Solution Structure of Crh, the Bacillus subtilis Catabolite Repression HPr'''
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===Solution Structure of Crh, the Bacillus subtilis Catabolite Repression HPr===
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==Overview==
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The solution structure and dynamics of the Bacillus subtilis HPr-like protein, Crh, have been investigated using NMR spectroscopy. Crh exhibits high sequence identity (45 %) to the histidine-containing protein (HPr), a phospho-carrier protein of the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system, but contains no catalytic His15, the site of PEP-dependent phosphorylation in HPr. Crh also forms a mixture of monomers and dimers in solution whereas HPr is known to be monomeric. Complete backbone and side-chain assignments were obtained for the monomeric form, and 60 % of the dimer backbone resonances; allowing the identification of the Crh dimer interface from chemical-shift mapping. The conformation of Crh was determined to a precision of 0.46(+/-0.06) A for the backbone atoms, and 1.01(+/-0.08) A for the heavy atoms. The monomer structure is similar to that of known HPr 2.67(+/-0.22) A (C(alpha) rmsd), but has a few notable differences, including a change in the orientation of one of the helices (B), and a two-residue shift in beta-sheet pairing of the N-terminal strand with the beta4 strand. This shift results in a shortening of the surface loop present in HPr and consequently provides a flatter surface in the region of dimerisation contact, which may be related to the different oligomeric nature of these two proteins. A binding site of phospho-serine(P-Ser)-Crh with catabolite control protein A (CcpA) is proposed on the basis of highly conserved surface side-chains between Crh and HPr. This binding site is consistent with the model of a dimer-dimer interaction between P-Ser-Crh and CcpA. (15)N relaxation measured in the monomeric form also identified differential local mobility in the helix B which is located in the vicinity of this site.
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(as it appears on PubMed at http://www.pubmed.gov), where 11916384 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11916384}}
==About this Structure==
==About this Structure==
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1K1C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K1C OCA].
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1K1C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K1C OCA].
==Reference==
==Reference==
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[[Category: Open-faced b-sandwich]]
[[Category: Open-faced b-sandwich]]
[[Category: Phosphotransferase system]]
[[Category: Phosphotransferase system]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:10:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 21:16:21 2008''

Revision as of 18:16, 1 July 2008

Image:1k1c.png

Template:STRUCTURE 1k1c

Solution Structure of Crh, the Bacillus subtilis Catabolite Repression HPr

Template:ABSTRACT PUBMED 11916384

About this Structure

1K1C is a Single protein structure of sequence from Bacillus subtilis. Full experimental information is available from OCA.

Reference

Solution structure and dynamics of Crh, the Bacillus subtilis catabolite repression HPr., Favier A, Brutscher B, Blackledge M, Galinier A, Deutscher J, Penin F, Marion D, J Mol Biol. 2002 Mar 15;317(1):131-44. PMID:11916384

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