3dsg

XC1028 from Xanthomonas campestris Adopts a PilZ Domain-like Structure Yet with Trivial c-di-GMP Binding Activity

spinqualitylabelsall models 3dsg, resolution 2.09Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3dsg is a 3 chain structure with sequence from Xanthomonas campestris pv. campestris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.09Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8PBU4_XANCP Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structure of XC1028 from Xanthomonas campestris has been determined to a resolution of 2.15 A using the multiple anomalous dispersion approach. It bears significant sequence identity and similarity values of 64.10% and 70.09%, respectively, with PA2960, a protein indispensable for type IV pilus-mediated twitching motility, after which the PilZ motif was first named. However, both XC1028 and PA2960 lack detectable c-di-GMP binding capability. Although XC1028 adopts a structure comprising a five-stranded beta-barrel core similar to other canonical PilZ domains with robust c-di-GMP binding ability, considerable differences are observed in the N-terminal motif; XC1028 assumes a compact five-stranded beta-barrel without an extra long N-terminal motif, whereas other canonical PilZ domains contain a long N-terminal sequence embedded with an essential "c-di-GMP switch" motif. In addition, a beta-strand (beta1) in the N-terminal motif, running in exactly opposite polarity to that of XC1028, is found inserted into the parallel beta3/beta1' strands, forming a completely antiparallel beta4 downward arrow beta3 upward arrow beta1 downward arrow beta1' upward arrow sheet in the canonical PilZ domains. Such dramatic structural differences at the N-terminus may account for the diminished c-di-GMP binding capability of XC1028, and suggest that interactions with additional proteins are necessary to bind c-di-GMP for type IV fimbriae assembly. XC1028 from Xanthomonas campestris adopts a PilZ domain-like structure without a c-di-GMP switch.,Li TN, Chin KH, Liu JH, Wang AH, Chou SH Proteins. 2009 May 1;75(2):282-8. PMID:19127589 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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