Protein Family Models

The hinge domain of chromosome partition protein MukB is responsible for dimerisation and is also involved in protein-DNA interactions and conformational flexibility [1]. [1]. 19853611. The crystal structure of the hinge domain of the Escherichia coli structural maintenance of chromosomes protein MukB. Li Y, Schoeffler AJ, Berger JM, Oakley MG;. J Mol Biol. 2010;395:11-19. (from Pfam)

Date:

2024-10-16

This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homologue SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains [1,2,3,4]. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region [4]. [1]. 26896444. Structural mechanism of ATP-dependent DNA binding and DNA end bridging by eukaryotic Rad50. Seifert FU, Lammens K, Stoehr G, Kessler B, Hopfner KP;. EMBO J. 2016;35:759-772. [2]. 21892167. The Rad50 coiled-coil domain is indispensable for Mre11 complex functions. Hohl M, Kwon Y, Galvan SM, Xue X, Tous C, Aguilera A, Sung P, Petrini JH;. Nat Struct Mol Biol. 2011;18:1124-1131. [3]. 28134932. Eukaryotic Rad50 functions as a rod-shaped dimer. Park YB, Hohl M, Padjasek M, Jeong E, Jin KS, Krezel A, Petrini JH, Cho Y;. Nat Struct Mol Biol. 2017;24:248-257. [4]. 31492634. Mechanism of DNA End Sensing and Processing by the Mre11-Rad50 Complex. Kashammer L, Saathoff JH, Lammens K, Gut F, Bartho J, Alt A, Kessler B, Hopfner KP;. Mol Cell. 2019;76:382-394. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

This family represents the N-terminal region of MukB, one of a group of bacterial proteins essential for the movement of nucleoids from mid-cell towards the cell quarters (i.e. chromosome partitioning). The structure of the N-terminal domain consists of an antiparallel six-stranded beta sheet surrounded by one helix on one side and by five helices on the other side [1]. It contains an exposed Walker A loop in an unexpected helix-loop-helix motif (in other proteins, Walker A motifs generally adopt a P loop conformation as part of a strand-loop-helix motif embedded in a conserved topology of alternating helices and (parallel) beta strands)[1]. [1]. 10545328. Crystal structure of the N-terminal domain of MukB: a protein involved in chromosome partitioning. van den Ent F, Lockhart A, Kendrick-Jones J, Lowe J;. Structure Fold Des 1999;7:1181-1187. (from Pfam)

Date:

2024-10-16

chromosome partition protein MukB is a structural maintenance of chromosome-like protein involved in chromosome condensation and partitioning

Date:

2019-04-13

SMC (structural maintenance of chromosomes) family of proteins; involved in chromosome condensatin and partitioning; forms a homodimer and the C-terminal is essential for DNA-binding activity while the purified N-terminal domain binds FtsZ

Gene:

mukB

Date:

2021-07-29