Structural highlights
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 PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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