1NIG

2.0 A Structure of Protein of Unknown Function from Thermoplasma acidophilum

1NIG の概要

• エントリーDOI: 10.2210/pdb1nig/pdb
• 分子名称: hypothetical protein TA1238 (2 entities in total)
• 機能のキーワード: structural genomics, four helixbundle, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function
• 由来する生物種: Thermoplasma acidophilum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17921.28

構造登録者

Sanishvili, R.,Edwards, A.,Christendat, D.,Midwest Center for Structural Genomics (MCSG) (登録日: 2002-12-23, 公開日: 2003-07-15, 最終更新日: 2024-04-03)

主引用文献

Sanishvili, R.,Pennycooke, M.,Gu, J.,Xu, X.,Joachimiak, A.,Edwards, A.M.,Christendat, D.
Crystal structure of the hypothetical protein TA1238 from Thermoplasma acidophilum: a new type of helical super-bundle.
J.STRUCT.FUNCT.GENOM., 5:231-240, 2004

PubMed Abstract: The crystal structure of the hypothetical protein TA1238 from Thermoplasma acidophilum was solved with multiple-wavelength anomalous diffraction and refined at 2.0 A resolution. The molecule consists of a typical four-helix antiparallel bundle with overhand connection. However, its oligomerization into a trimer leads to a coiled "super-helix" which is novel for such bundles. Its central feature, a six-stranded coiled coil, is also novel for proteins. TA1238 does not have strong sequence homologues in databases, but shows strong structural similarity with some proteins in the Protein Data Bank. The function could not be inferred from the sequence but the structure, with some rearrangement, bears some resemblance to the active site region of cobalamin adenosyltransferase (TA1434). Specifically, TA1238 retains Arg104, which is structurally equivalent to functionally critical Arg119 of TA1434. For such conformational change, the overhand connection of TA1238 might need to be involved in a gating mechanism that might be modulated by ligands and/or by interactions with the physiological partners. This allowed us to hypothesize that TA1238 could be involved in cobalamin biosyntheses.

PubMed: 15704011
DOI: 10.1007/s10969-005-3789-1

実験手法

X-RAY DIFFRACTION (2 Å)