Structure of the full-length yeast Arp7–Arp9 heterodimer

2014 ◽  
Vol 70 (2) ◽  
pp. 310-316 ◽  
Author(s):  
Joel Lobsiger ◽  
Yvonne Hunziker ◽  
Timothy J. Richmond
Keyword(s):  
Crystal Structure ◽  
Regulatory Protein ◽  
Chromatin Remodelling ◽  
Full Length ◽  
Nuclear Actin ◽  
Dimerization Interface ◽  
Related Proteins

The nuclear actin-related proteins Arp7 and Arp9 are components of the yeast SWI/SNF and RSC chromatin-remodelling complexes. The 3.1 Å resolution crystal structure reported here shows that the full-length Arp7 and Arp9 proteins exist as a dimer without a requirement for additional polypeptides. Of the 11 actin-related proteins, Arp7 and Arp9 are the only two directly demonstrated to form a dimer within this family. The Arp7–Arp9 heterodimer is unlikely to form an actin-like filament based on modelling using the structure. The Arp7–Arp9 structure reveals that its dimerization interface is not altered when bound in a complex with the SWI/SNF Snf2 HSA domain and the regulatory protein Rtt102.

scholarly journals The crystal structure of full-length Sizzled fromXenopus laevisyields insights into Wnt-antagonistic function of secreted Frizzled-related proteins

2017 ◽  
Vol 292 (39) ◽  
pp. 16055-16069 ◽  
Author(s):  
Qixin Bu ◽  
Zhiqiang Li ◽  
Junying Zhang ◽  
Fei Xu ◽  
Jianmei Liu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Full Length ◽  
Related Proteins

scholarly journals Global versus Local Regulatory Roles for Lrp-Related Proteins: Haemophilus influenzae as a Case Study

2001 ◽  
Vol 183 (13) ◽  
pp. 4004-4011 ◽  
Author(s):  
Devorah Friedberg ◽  
Michael Midkiff ◽  
Joseph M. Calvo
Keyword(s):  
Amino Acid ◽  
Haemophilus Influenzae ◽  
Regulatory Protein ◽  
Enteric Bacteria ◽  
Regulatory Role ◽  
Regulatory Function ◽  
Ecological Niches ◽  
E Coli ◽  
Sequence Identity ◽  
Related Proteins

ABSTRACT Lrp (leucine-responsive regulatory protein) plays a global regulatory role in Escherichia coli, affecting expression of dozens of operons. Numerous lrp-related genes have been identified in different bacteria and archaea, includingasnC, an E. coli gene that was the first reported member of this family. Pairwise comparisons of amino acid sequences of the corresponding proteins shows an average sequence identity of only 29% for the vast majority of comparisons. By contrast, Lrp-related proteins from enteric bacteria show more than 97% amino acid identity. Is the global regulatory role associated withE. coli Lrp limited to enteric bacteria? To probe this question we investigated LrfB, an Lrp-related protein fromHaemophilus influenzae that shares 75% sequence identity with E. coli Lrp (highest sequence identity among 42 sequences compared). A strain of H. influenzae having anlrfB null allele grew at the wild-type growth rate but with a filamentous morphology. A comparison of two-dimensional (2D) electrophoretic patterns of proteins from parent and mutant strains showed only two differences (comparable studies withlrp + and lrp E. coli strains by others showed 20 differences). The abundance of LrfB in H. influenzae, estimated by Western blotting experiments, was about 130 dimers per cell (compared to 3,000 dimers per E. colicell). LrfB expressed in E. coli replaced Lrp as a repressor of the lrp gene but acted only to a limited extent as an activator of the ilvIH operon. Thus, although LrfB resembles Lrp sufficiently to perform some of its functions, its low abundance is consonant with a more local role in regulating but a few genes, a view consistent with the results of the 2D electrophoretic analysis. We speculate that an Lrp having a global regulatory role evolved to help enteric bacteria adapt to their ecological niches and that it is unlikely that Lrp-related proteins in other organisms have a broad regulatory function.

Crystal Structure of Full Length Topoisomerase I from Thermotoga maritima

2006 ◽  
Vol 358 (5) ◽  
pp. 1328-1340 ◽  
Author(s):  
Guido Hansen ◽  
Axel Harrenga ◽  
Bernd Wieland ◽  
Dietmar Schomburg ◽  
Peter Reinemer
Keyword(s):  
Crystal Structure ◽  
Topoisomerase I ◽  
Thermotoga Maritima ◽  
Full Length

scholarly journals Structure of the N-terminal dimerization domain of CEACAM7

2015 ◽  
Vol 71 (9) ◽  
pp. 1169-1175 ◽  
Author(s):  
Daniel A. Bonsor ◽  
Dorothy Beckett ◽  
Eric J. Sundberg
Keyword(s):  
Crystal Structure ◽  
Hydrogen Bond ◽  
Sequence Variation ◽  
Cellular Adhesion ◽  
Sedimentation Equilibrium ◽  
Colorectal Cancers ◽  
Dimerization Domain ◽  
Adhesion Protein ◽  
Dimerization Interface ◽  
Colon And Rectum

CEACAM7 is a human cellular adhesion protein that is expressed on the surface of colon and rectum epithelial cells and is downregulated in colorectal cancers. It achieves cell adhesion through dimerization of the N-terminal IgV domain. The crystal structure of the N-terminal dimerization domain of CEACAM has been determined at 1.47 Å resolution. The overall fold of CEACAM7 is similar to those of CEACAM1 and CEACAM5; however, there are differences, the most notable of which is an insertion that causes theC′′ strand to buckle, leading to the creation of a hydrogen bond in the dimerization interface. TheKdimerizationfor CEACAM7 determined by sedimentation equilibrium is tenfold tighter than that measured for CEACAM5. These findings suggest that the dimerization affinities of CEACAMs are modulatedviasequence variation in the dimerization surface.

Peroxisomal multifunctional enzyme type 2 from the fruitfly: dehydrogenase and hydratase act as separate entities, as revealed by structure and kinetics

2011 ◽  
Vol 435 (3) ◽  
pp. 771-781 ◽  
Author(s):  
Tatu J. K. Haataja ◽  
M. Kristian Koski ◽  
J. Kalervo Hiltunen ◽  
Tuomo Glumoff
Keyword(s):  
Crystal Structure ◽  
Saccharomyces Cerevisiae ◽  
Drosophila Melanogaster ◽  
Structural Features ◽  
Full Length ◽  
Multifunctional Enzyme ◽  
Domain Composition ◽  
Substrate Channelling

All of the peroxisomal β-oxidation pathways characterized thus far house at least one MFE (multifunctional enzyme) catalysing two out of four reactions of the spiral. MFE type 2 proteins from various species display great variation in domain composition and predicted substrate preference. The gene CG3415 encodes for Drosophila melanogaster MFE-2 (DmMFE-2), complements the Saccharomyces cerevisiae MFE-2 deletion strain, and the recombinant protein displays both MFE-2 enzymatic activities in vitro. The resolved crystal structure is the first one for a full-length MFE-2 revealing the assembly of domains, and the data can also be transferred to structure–function studies for other MFE-2 proteins. The structure explains the necessity of dimerization. The lack of substrate channelling is proposed based on both the structural features, as well as by the fact that hydration and dehydrogenation activities of MFE-2, if produced as separate enzymes, are equally efficient in catalysis as the full-length MFE-2.

scholarly journals Structural analysis of point mutations at theVaccinia virusA20/D4 interface

2016 ◽  
Vol 72 (9) ◽  
pp. 687-691 ◽  
Author(s):  
Céline Contesto-Richefeu ◽  
Nicolas Tarbouriech ◽  
Xavier Brazzolotto ◽  
Wim P. Burmeister ◽  
Christophe N. Peyrefitte ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acids ◽  
Structural Analysis ◽  
Complex Formation ◽  
Dna Polymerase ◽  
Point Mutations ◽  
Conformational Space ◽  
Uracil Dna Glycosylase ◽  
Dimerization Interface ◽  
Solvation Parameters

TheVaccinia viruspolymerase holoenzyme is composed of three subunits: E9, the catalytic DNA polymerase subunit; D4, a uracil-DNA glycosylase; and A20, a protein with no known enzymatic activity. The D4/A20 heterodimer is the DNA polymerase cofactor, the function of which is essential for processive DNA synthesis. The recent crystal structure of D4 bound to the first 50 amino acids of A20 (D4/A201–50) revealed the importance of three residues, forming a cation–π interaction at the dimerization interface, for complex formation. These are Arg167 and Pro173 of D4 and Trp43 of A20. Here, the crystal structures of the three mutants D4-R167A/A201–50, D4-P173G/A201–50and D4/A201–50-W43A are presented. The D4/A20 interface of the three structures has been analysed for atomic solvation parameters and cation–π interactions. This study confirms previous biochemical data and also points out the importance for stability of the restrained conformational space of Pro173. Moreover, these new structures will be useful for the design and rational improvement of known molecules targeting the D4/A20 interface.

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