NDLI: Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Serrano, Pedro Pedrini, Bill Geralt, Michael Jaudzems, Kristaps Mohanty, Biswaranjan Horst, Reto Herrmann, Torsten Elsliger, Marc André Wilson, Ian A. Wüthrich, Kurt
Description	Country affiliation: United States Author Affiliation: Serrano P ( Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.)
Abstract	The JCSG has recently developed a protocol for systematic comparisons of high-quality crystal and NMR structures of proteins. In this paper, the extent to which this approach can provide function-related information on the two functionally annotated proteins TM1081, a Thermotoga maritima anti-σ factor antagonist, and A2LD1 (gi:13879369), a mouse Î³-glutamylamine cyclotransferase, is explored. The NMR structures of the two proteins have been determined in solution at 313 and 298âK, respectively, using the current JCSG protocol based on the software package UNIO for extensive automation. The corresponding crystal structures were solved by the JCSG at 100âK and 1.6âÅ resolution and at 100âK and 1.9âÅ resolution, respectively. The NMR and crystal structures of the two proteins share the same overall molecular architectures. However, the precision of the structure determination along the amino-acid sequence varies over a significantly wider range in the NMR structures than in the crystal structures. Thereby, in each of the two NMR structures about 65% of the residues have displacements below the average and in both proteins the less well ordered residues include large parts of the active sites, in addition to some highly solvent-exposed surface areas. Whereas the latter show increased disorder in the crystal and in solution, the active-site regions display increased displacements only in the NMR structures, where they undergo local conformational exchange on the millisecond time scale that appears to be frozen in the crystals. These observations suggest that a search for molecular regions showing increased structural disorder and slow dynamic processes in solution while being well ordered in the corresponding crystal structure might be a valid initial step in the challenge of identifying putative active sites in functionally unannotated proteins with known three-dimensional structure.
File Format	HTM / HTML
ISSN	2053230X
e-ISSN	17443091
DOI	10.1107/S1744309110033658
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Issue Number	Pt 10
Volume Number	66
Language	English
Publisher	Wiley
Publisher Date	2010-10-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Crystallography Discipline Biophysics Discipline Molecular Biology Discipline Biochemistry Bacterial Proteins Catalytic Domain Thermotoga Maritima Chemistry Amino Acid Sequence Binding Sites Crystallography, X-ray Isomerism Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Proteins Comparative Study Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s.
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics

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