1a04

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[[Category: two-component systems]]
[[Category: two-component systems]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:22:15 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:43:38 2007''

Revision as of 12:38, 30 October 2007


1a04, resolution 2.2Å

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THE STRUCTURE OF THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL IN THE MONOCLINIC C2 CRYSTAL FORM

Overview

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, ... [(full description)]

About this Structure

1A04 is a [Single protein] structure of sequence from [Escherichia coli]. Structure known Active Site: 1. Full crystallographic information is available from [OCA].

Reference

NarL dimerization? Suggestive evidence from a new crystal form., Baikalov I, Schroder I, Kaczor-Grzeskowiak M, Cascio D, Gunsalus RP, Dickerson RE, Biochemistry. 1998 Mar 17;37(11):3665-76. PMID:9521685

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