Document Detail

NarL dimerization? Suggestive evidence from a new crystal form.
MedLine Citation:
PMID:  9521685     Owner:  NLM     Status:  MEDLINE    
The structure of the Escherichia coli response regulator NarL has been solved in a new, monoclinic space group, and compared with the earlier orthorhombic crystal structure. Because the monoclinic crystal has two independent NarL molecules per asymmetric unit, we now have three completely independent snapshots of the NarL molecule: two from the monoclinic form and one from the orthorhombic. Comparison of these three structures shows the following: (a) The pairing of N and C domains of the NarL molecule proposed from the earlier analysis is in fact correct, although the polypeptide chain connecting domains was, and remains, disordered and not completely visible. The new structure exhibits identical relative orientation of N and C domains, and supplies some of the missing residues, leaving a gap of only seven amino acids. (b) Examination of corresponding features in the three independent NarL molecules shows that deformations in structure produced by crystal packing are negligible. (c) The "telephone receiver" model of NarL activation is confirmed. The N domain of NarL blocks the binding of DNA to the C domain that would be expected from the helix-turn-helix structure of the C domain. Hence, binding can only occur after significant displacement of N and C domains. (d) NarL monomers have a strong tendency toward dimerization involving contacts between helixes alpha 1 in the two monomers, and this may have mechanistic significance in DNA binding. Analogous involvement of helix alpha 1 in intermolecular contacts is also found in UhpA and in the CheY/CheZ complex.
I Baikalov; I Schröder; M Kaczor-Grzeskowiak; D Cascio; R P Gunsalus; R E Dickerson
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  37     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1998 Mar 
Date Detail:
Created Date:  1998-04-14     Completed Date:  1998-04-14     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  3665-76     Citation Subset:  IM    
Molecular Biology Institute, University of California, Los Angeles 90095-1570, USA.
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MeSH Terms
Amino Acid Sequence
Bacterial Proteins / chemistry*
Crystallography, X-Ray
DNA-Binding Proteins / chemistry*
Escherichia coli
Escherichia coli Proteins*
Models, Molecular
Molecular Sequence Data
Protein Structure, Secondary
Protein Structure, Tertiary
Structure-Activity Relationship
Reg. No./Substance:
0/Bacterial Proteins; 0/DNA-Binding Proteins; 0/Escherichia coli Proteins; 123940-13-6/NarL protein, E coli

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