1qzm
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The crystal structure of the small, mostly helical alpha domain of the | + | 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== | ==About this Structure== | ||
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[[Category: Cherry, S.]] | [[Category: Cherry, S.]] | ||
[[Category: Gustchina, A.]] | [[Category: Gustchina, A.]] | ||
| - | [[Category: Khalatova, A | + | [[Category: Khalatova, A G.]] |
| - | [[Category: Maurizi, M | + | [[Category: Maurizi, M R.]] |
| - | [[Category: Melnikov, E | + | [[Category: Melnikov, E E.]] |
| - | [[Category: Rasulova, F | + | [[Category: Rasulova, F S.]] |
| - | [[Category: Rotanova, T | + | [[Category: Rotanova, T V.]] |
| - | [[Category: Tropea, J | + | [[Category: Tropea, J E.]] |
[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
[[Category: aaa+ protein]] | [[Category: aaa+ protein]] | ||
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[[Category: oligomerization domain]] | [[Category: oligomerization domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:31 2008'' |
Revision as of 12:45, 21 February 2008
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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. Active as Endopeptidase La, with EC number 3.4.21.53 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
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