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1H and15N NMR resonance assignments and solution secondary structure of oxidizedDesulfovibrio desulfuricansflavodoxin

✍ Scribed by John R. Pollock; Richard P. Swenson; Brian J. Stockman

Publisher
Springer Netherlands
Year
1996
Tongue
English
Weight
839 KB
Volume
7
Category
Article
ISSN
0925-2738

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✦ Synopsis

Sequence-specific ~H and ~SN resonance assignments have been made for 137 of the 146 nonprolyl residues in oxidized Desulfovibrio desulfuricans [Essex 6] flavodoxin. Assignments were obtained by a concerted analysis of the heteronuclear three-dimensional ~H-~SN NOESY-HMQC and TOCSY-HMQC data sets, recorded on uniformly ~SN-enriched protein at 300 K. Numerous side-chain resonances have been partially or fully assigned. Residues with overlapping ~H TM chemical shifts were resolved by a threedimensional tH-~N HMQC-NOESY-HMQC spectrum. Medium-and long-range NOEs, 3JNHa coupling constants, and ~H TM exchange data indicate a secondary structure consisting of five parallel t-strands and four m-helices with a topology similar to that of Desulfovibrio vulgaris [Hildenborough] flavodoxin. Prolines at positions 106 and 134, which are not conserved in D. vulgaris flavodoxin, contort the two C-terminal c~-helices.

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