2jqx
From Proteopedia
(New page: 200px<br /><applet load="2jqx" size="450" color="white" frame="true" align="right" spinBox="true" caption="2jqx" /> '''Solution structure of Malate Synthase G from...) |
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'''Solution structure of Malate Synthase G from joint refinement against NMR and SAXS data'''<br /> | '''Solution structure of Malate Synthase G from joint refinement against NMR and SAXS data'''<br /> | ||
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| + | ==Overview== | ||
| + | Determination of the accurate three-dimensional structure of large, proteins by NMR remains challenging due to a loss in the density of, experimental restraints resulting from the often prerequisite, perdeuteration. Solution small-angle scattering, which carries long-range, translational information, presents an opportunity to enhance the, structural accuracy of derived models when used in combination with global, orientational NMR restraints such as residual dipolar couplings (RDCs) and, residual chemical shift anisotropies (RCSAs). We have quantified the, improvements in accuracy that can be obtained using this strategy for the, 82 kDa enzyme Malate Synthase G (MSG), currently the largest single chain, protein solved by solution NMR. Joint refinement against NMR and, scattering data leads to an improvement in structural accuracy as, evidenced by a decrease from approximately 4.5 to approximately 3.3 A of, the backbone rmsd between the derived model and the high-resolution X-ray, structure, PDB code 1D8C. This improvement results primarily from, medium-angle scattering data, which encode the overall molecular shape, rather than the lowest angle data that principally determine the radius of, gyration and the maximum particle dimension. The effect of the higher, angle data, which are dominated by internal density fluctuations, while, beneficial, is also found to be relatively small. Our results demonstrate, that joint NMR/SAXS refinement can yield significantly improved accuracy, in solution structure determination and will be especially well suited for, the study of systems with limited NMR restraints such as large proteins, oligonucleotides, or their complexes. | ||
==About this Structure== | ==About this Structure== | ||
| - | 2JQX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Malate_synthase Malate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.9 2.3.3.9] Full crystallographic information is available from [http:// | + | 2JQX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Malate_synthase Malate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.9 2.3.3.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JQX OCA]. |
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| + | ==Reference== | ||
| + | Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints., Grishaev A, Tugarinov V, Kay LE, Trewhella J, Bax A, J Biomol NMR. 2008 Feb;40(2):95-106. Epub 2007 Nov 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18008171 18008171] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Malate synthase]] | [[Category: Malate synthase]] | ||
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[[Category: small-angle x-ray scattering]] | [[Category: small-angle x-ray scattering]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 10:39:16 2008'' |
Revision as of 08:39, 23 January 2008
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Solution structure of Malate Synthase G from joint refinement against NMR and SAXS data
Overview
Determination of the accurate three-dimensional structure of large, proteins by NMR remains challenging due to a loss in the density of, experimental restraints resulting from the often prerequisite, perdeuteration. Solution small-angle scattering, which carries long-range, translational information, presents an opportunity to enhance the, structural accuracy of derived models when used in combination with global, orientational NMR restraints such as residual dipolar couplings (RDCs) and, residual chemical shift anisotropies (RCSAs). We have quantified the, improvements in accuracy that can be obtained using this strategy for the, 82 kDa enzyme Malate Synthase G (MSG), currently the largest single chain, protein solved by solution NMR. Joint refinement against NMR and, scattering data leads to an improvement in structural accuracy as, evidenced by a decrease from approximately 4.5 to approximately 3.3 A of, the backbone rmsd between the derived model and the high-resolution X-ray, structure, PDB code 1D8C. This improvement results primarily from, medium-angle scattering data, which encode the overall molecular shape, rather than the lowest angle data that principally determine the radius of, gyration and the maximum particle dimension. The effect of the higher, angle data, which are dominated by internal density fluctuations, while, beneficial, is also found to be relatively small. Our results demonstrate, that joint NMR/SAXS refinement can yield significantly improved accuracy, in solution structure determination and will be especially well suited for, the study of systems with limited NMR restraints such as large proteins, oligonucleotides, or their complexes.
About this Structure
2JQX is a Single protein structure of sequence from Escherichia coli. Active as Malate synthase, with EC number 2.3.3.9 Full crystallographic information is available from OCA.
Reference
Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints., Grishaev A, Tugarinov V, Kay LE, Trewhella J, Bax A, J Biomol NMR. 2008 Feb;40(2):95-106. Epub 2007 Nov 16. PMID:18008171
Page seeded by OCA on Wed Jan 23 10:39:16 2008
Categories: Escherichia coli | Malate synthase | Single protein | Bax, A. | Grishaev, A. | Kay, L.E. | Trewhella, J. | Tugarinov, V. | 82 kda enzyme | Alignment | Apo-malate synthase g | Deuteration | Rdc | Residual chemical shift anisotropy | Residual dipolar coupling | Saxs | Small-angle x-ray scattering
