5vaw

Fusion of Maltose-binding Protein and PilA from Acinetobacter baumannii AB5075

spinqualitylabelsall models 5vaw, resolution 1.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5vaw is a 1 chain structure with sequence from Acinetobacter baumannii and Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.69Å Ligands: GLU, LYS, MPD, NA, SER Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.A0A0D5YCX7_ACIBA Publication Abstract from PubMed Type IV pili (T4P) are bacterial appendages composed of protein subunits, called pilins, non-covalently assembled into helical fibers. T4P are essential, in many bacterial species, for processes as diverse as twitching motility, natural competence, biofilm or microcolony formation, and host-cell adhesion. The genes encoding type IV pili are found universally in the Gram-negative, aerobic, non-flagellated, and pathogenic coccobacillus Acinetobacter baumannii, but there is considerable variation in PilA, the major protein subunit, both in amino acid sequence and glycosylation patterns. Here we report the X-tray crystal structure of PilA from AB5075, a recently-characterized, highly-virulent isolate, at 1.9A resolution and compare it to homologues from A. baumannii strains ACICU and BIDMC57, which are C-terminally-glycosylated. These structural comparisons revealed that PilA(AB5075) exhibits a distinctly electronegative surface chemistry. To understand the functional consequences of this change in surface electrostatics, we complemented a DeltapilA knockout strain with divergent pilA genes from ACICU, BIDMC57 and AB5075. The resulting transgenic strains showed differential twitching motility and biofilm formation while maintaining the ability to adhere to epithelial cells. PilA(AB5075) and PilA(ACICU), while structurally similar, promote different characteristics, favoring twitching motility and biofilm formation respectively. These results support a model in which differences in pilus electrostatics affect the equilibrium of microcolony formation, which in turn alters the balance between motility and biofilm formation in Acinetobacter. The Structure of PilA from Acinetobacter baumannii AB5075 suggests a mechanism for functional specialization in Acinetobacter type IV pili.,Ronish LA, Lillehoj E, Fields JK, Sundberg EJ, Piepenbrink KH J Biol Chem. 2018 Nov 9. pii: RA118.005814. doi: 10.1074/jbc.RA118.005814. PMID:30413536 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA