1qzm
From Proteopedia
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| , resolution 1.90Å | |||||||
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| Gene: | LON (Escherichia coli) | ||||||
| Activity: | Endopeptidase La, with EC number 3.4.21.53 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
alpha-domain of ATPase
Overview
The crystal structure of the small, mostly helical alpha domain of the AAA+ module of the Escherichia coli ATP-dependent protease Lon has been solved by single isomorphous replacement combined with anomalous scattering and refined at 1.9A resolution to a crystallographic R factor of 17.9%. This domain, comprising residues 491-584, was obtained by chymotrypsin digestion of the recombinant full-length protease. The alpha domain of Lon contains four alpha helices and two parallel strands and resembles similar domains found in a variety of ATPases and helicases, including the oligomeric proteases HslVU and ClpAP. The highly conserved "sensor-2" Arg residue is located at the beginning of the third helix. Detailed comparison with the structures of 11 similar domains established the putative location of the nucleotide-binding site in this first fragment of Lon for which a crystal structure has become available.
About this Structure
1QZM is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution., Botos I, Melnikov EE, Cherry S, Khalatova AG, Rasulova FS, Tropea JE, Maurizi MR, Rotanova TV, Gustchina A, Wlodawer A, J Struct Biol. 2004 Apr-May;146(1-2):113-22. PMID:15037242
Page seeded by OCA on Thu Mar 20 13:44:50 2008
