2XT2

Structure of the pentapeptide repeat protein AlbG, a resistance factor for the topoisomerase poison albicidin.

2XT2 の概要

• エントリーDOI: 10.2210/pdb2xt2/pdb
• 分子名称: MCBG-LIKE PROTEIN, SULFATE ION (3 entities in total)
• 機能のキーワード: cell cycle, right handed quadrilateral beta helix
• 由来する生物種: XANTHOMONAS ALBILINEANS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45929.41

構造登録者

Vetting, M.W.,Hegde, S.S.,Blanchard, J.S. (登録日: 2010-10-05, 公開日: 2010-10-13, 最終更新日: 2024-05-08)

主引用文献

Vetting, M.W.,Hegde, S.S.,Zhang, Y.,Blanchard, J.S.
Pentapeptide-Repeat Proteins that Act as Topoisomerase Poison Resistance Factors Have a Common Dimer Interface.
Acta Crystallogr.,Sect.F, 67:296-, 2011

PubMed Abstract: The protein AlbG is a self-resistance factor against albicidin, a nonribosomally encoded hybrid polyketide-peptide with antibiotic and phytotoxic properties produced by Xanthomonas albilineans. Primary-sequence analysis indicates that AlbG is a member of the pentapeptide-repeat family of proteins (PRP). The structure of AlbG from X. albilineans was determined at 2.0 Å resolution by SAD phasing using data collected from a single trimethyllead acetate derivative on a home source. AlbG folds into a right-handed quadrilateral β-helix composed of approximately eight semi-regular coils. The regularity of the β-helix is blemished by a large loop/deviation in the β-helix between coils 4 and 5. The C-terminus of the β-helix is capped by a dimerization module, yielding a dimer with a 110 Å semi-collinear β-helical axis. This method of dimer formation appears to be common to all PRP proteins that confer resistance to topoisomerase poisons and contrasts with most PRP proteins, which are typically monomeric.

PubMed: 21393830
DOI: 10.1107/S1744309110053315

実験手法

X-RAY DIFFRACTION (1.999 Å)