2XT4

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

Summary for 2XT4

• Entry DOI: 10.2210/pdb2xt4/pdb
• Related: 2XT2
• Descriptor: MCBG-LIKE PROTEIN (2 entities in total)
• Functional Keywords: cell cycle, right handed quadrilateral beta helix
• Biological source: XANTHOMONAS ALBILINEANS
• Total number of polymer chains: 2
• Total formula weight: 43969.26

Authors

Vetting, M.W.,Hegde, S.S.,Blanchard, J.S. (deposition date: 2010-10-05, release date: 2010-10-13, Last modification date: 2023-12-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.394 Å)