2.5 A resolution crystal structure of the motile major sperm protein (MSP) of Ascaris suum

Journal of Molecular Biology
T L BullockM Stewart

Abstract

We have determined the structure of the Ascaris major sperm protein (MSP) to 2.5 A resolution using X-ray crystallography. The MSP polypeptide chain has an immunoglobulin-like fold based on a seven-stranded beta sandwich. In two strands, cis-proline residues impart distinctive kinks, and overall the structure most closely resembles that of the N-terminal domain of the bacterial chaperonin, PapD. In the C2 crystal form which we have solved here, two MSP chains are tightly associated in the asymmetric unit and are related by a non-crystallographic 2-fold rotation axis. This arrangement almost certainly represents the MSP dimer that is present in solution. Additionally, the arrangement of two MSP dimers at one of the crystallographic 2-fold axes in the 215 A unit cell suggests a possible mode for the assembly of MSP into the filaments which promote cell movement. This dimer-dimer association is based on a beta sheet extension mechanism between adjoining MSP monomers which resembles the interaction between PapD and its protein substrate.

Citations

Mar 21, 1998·Nature Structural Biology·T L BullockM Stewart
Jun 29, 2011·Proceedings of the National Academy of Sciences of the United States of America·Ellen L BatchelderJulie Plastino
Feb 3, 2000·Proceedings of the National Academy of Sciences of the United States of America·P A SkehelE R Kandel
Feb 20, 2007·Journal of Molecular Biology·Colin J JacksonDavid L Ollis
Jul 18, 2008·Bioorganic & Medicinal Chemistry·Junguk ParkKim D Janda
Jun 24, 2004·Proteins·Lizbeth L VideauJane S Richardson
Nov 21, 2007·Journal of Cellular Biochemistry·Antonio del Castillo-Olivares, Harold E Smith
Nov 10, 2007·Journal of Structural and Functional Genomics·Harold E Smith
Dec 25, 2009·Developmental Dynamics : an Official Publication of the American Association of Anatomists·Sung Min HanMichael A Miller
Nov 11, 2014·New Journal of Physics·Svitlana HavrylenkoJulie Plastino
Jan 27, 2016·Experimental Cell Research·Angie Darbyson, Johnny K Ngsee
Mar 29, 2000·Biochemical and Biophysical Research Communications·F LaurentP de Wit
Aug 21, 2001·Biochemical and Biophysical Research Communications·M L WeirW S Trimble
Jul 29, 2004·Molecular and Biochemical Parasitology·D E K Tarr, Alan L Scott
Jan 25, 2005·Biophysical Journal·Charles W WolgemuthGeorge Oster
Mar 10, 2005·Journal of Molecular Biology·Richard P GrantMurray Stewart
Jul 12, 2005·Structure·Stephen E KaiserAxel T Brunger
Jan 30, 2008·Biophysical Journal·Mark ZajacCharles W Wolgemuth
Oct 27, 2004·Biochemistry·James G Bann, Carl Frieden
Mar 21, 2001·Science·A M Villeneuve
Aug 5, 2009·Biophysical Journal·Jelena Stajic, Charles W Wolgemuth
Apr 13, 2010·Developmental Biology·Youfeng YangMichael A Miller

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