Structural and functional analysis of AsbF: Origin of the stealth 3,4-dihydroxybenzoic acid subunit for petrobactin biosynthesis

Proceedings of the National Academy of Sciences of the United States of America

Volumn 105, Issue 44, 2008, Pages 17133-17138

  Pfleger, Brian F ^a   Kim, Youngchang ^b   Nusca, Tyler D ^a,d   Maltseva, Natalia ^b   Jung, Yeop Lee ^a   Rath, Christopher M ^a   Scaglione, Jamie B ^a   Janes, Brian K ^d   Anderson, Erica C ^d   Bergman, Nicholas H ^e   Hanna, Philip C ^d   Joachimiak, Andrzej ^b,c   Sherman, David H ^a,d  

^a UNIVERSITY OF MICHIGAN   (United States)

^b ARGONNE NATIONAL LABORATORY   (United States)

^c UNIVERSITY OF CHICAGO   (United States)

^d UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^e GEORGIA TECH RESEARCH INSTITUTE   (United States)

Author keywords

AsbF structure; Dehydratase; Siderophore; Virulence factor

Indexed keywords

3 DEHYDROSHIKIMATE; BENZOIC ACID; DIHYDROBENZOIC ACID; HYDROLYASE; PETROBACTIN; PROTEIN ASBF; SHIKIMIC ACID DERIVATIVE; SIDEROPHORE; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS ANTHRACIS; BACTERIAL VIABILITY; CRYSTAL STRUCTURE; NONHUMAN; OPERON; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS;

ANIMALS; BACILLUS ANTHRACIS; BACTERIAL PROTEINS; BENZAMIDES; CRYSTALLOGRAPHY, X-RAY; HYDRO-LYASES; HYDROGEN-ION CONCENTRATION; HYDROXYBENZOIC ACIDS; MICE; MODELS, MOLECULAR; OPERON; PROTEIN CONFORMATION; SHIKIMIC ACID; STRUCTURE-ACTIVITY RELATIONSHIP;

BACILLUS ANTHRACIS; BACTERIA (MICROORGANISMS);

EID: 55949087762     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0808118105     Document Type: Article

References (43)

1. Andrews SC, Robinson AK, Rodriguez-Quinones F (2003) Bacterial iron homeostasis. FEMS Microbiol Rev 27:215-237.
2. Koppisch AT, et al. (2005) Petrobactin is the primary siderophore synthesized by Bacillus anthracis str. Sterne under conditions of iron starvation. Biometals 18:577-585.
3. Lee JY, et al. (2007) Biosynthetic analysis of the petrobactin siderophore pathway from Bacillus anthracis. J Bacteriol 189:1698-1710.
4. Wilson MK, Abergel RJ, Raymond KN, Arceneaux JE, Byers BR (2006) Siderophores of Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis. Biochem Biophys Res Commun 348:320-325.
5. Cendrowski S, MacArthur W, Hanna P (2004) Bacillus anthracis requires siderophore biosynthesis for growth in macrophages and mouse virulence. Mol Microbiol 51:407-417.
6. Koppisch AT, et al. (2008) Petrobactin is produced by both pathogenic and nonpathogenic isolates of the Bacillus cereus group of bacteria. Biometals 21:581-589.
7. Abergel RJ, et al. (2006) Anthrax pathogen evades the mammalian immune system through stealth siderophore production. Proc Natl Acad Sci USA 103:18499-18503.
8. Fischbach MA, Lin H, Liu DR, Walsh CT (2006) How pathogenic bacteria evade mammalian sabotage in the battle for iron. Nat Chem Biol 2:132-138.
9. Pfleger BF, et al. (2007) Characterization and analysis of early enzymes for petrobactin biosynthesis in Bacillus anthracis. Biochemistry 46:4147-4157.
10. Garner BL, Arceneaux JE, Byers BR (2004) Temperature control of a 3,4-dihydroxybenzoate (protocatechuate)-based siderophore in Bacillus anthracis. Curr Microbiol 49:89-94.
11. Koppisch AT, et al. (2008) Biosynthesis of the 3,4-dihydroxybenzoate moieties of petrobactin by Bacillus anthracis. J Org Chem 73:5759-5765.
12. Fisher N, et al. (2006) The dltABCD operon of Bacillus anthracis Sterne is required for virulence and resistance to peptide, enzymatic, and cellular mediators of innate immunity. J Bacteriol 188:1301-1309.
13. Hosokawa K, Stanier RY (1966) Crystallization and properties of p-hydroxybenzoate hydroxylase from Pseudomonas putida. J Biol Chem 241:2453-2460.
14. Frost JW, Draths KM (1995) Biocatalytic syntheses of aromatics from D-glucose: Renewable microbial sources of aromatic compounds. Annu Rev Microbiol 49:557-579.
15. Stroman P, Reinert WR, Giles NH (1978) Purification and characterization of 3-dehydroshikimate dehydratase, an enzyme in the inducible quinic acid catabolic pathway of Neurospora crassa. J Biol Chem 253:4593- 4598.
16. Wheeler KA, Lamb HK, Hawkins AR (1996) Control of metabolic flux through the quinate pathway in Aspergillus nidulans. Biochem J 315:195-205.
17. Yi J, Li K, Draths KM, Frost JW (2002) Modulation of phosphoenolpyruvate synthase expression increases shikimate pathway product yields in E. coli. Biotechnol Prog 18:1141-1148.
18. Fuxreiter M, Farkas O, Naray-Szabo G (1995) Molecular modelling of xylose isomerase catalysis: The role of electrostatics and charge transfer to metals. Protein Eng 8:925-933.
19. Gourley DG, et al. (1999) The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction. Nat Struct Biol 6:521-525.
20. Zhang RG, et al. (2002) Crystal structure of Bacillus subtilis loll shows endonuclase IV fold with altered Zn binding. Proteins 48:423-426.
21. Zheng H, Chruszcz M, Lasota P, Lebioda L, Minor W (2008) Data mining of metal ion environments present in protein structures. J Inorg Biochem 102:1765-1776.
22. Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372:774-797.
23. Deka RK, Kleanthous C, Coggins JR (1992) Identification of the essential histidine residue at the active site of Escherichia coli dehydroquinase. J Biol Chem 267:22237-22242.
24. 13CNMR. J Biol Chem 273:9602-9607.
25. Abergel RJ, Zawadzka AM, Raymond KN (2008) Petrobactin-mediated iron transport in pathogenic bacteria: Coordination chemistry of an unusual 3,4-catecholate/citrate siderophore. J Am Chem Soc 130:2124-2125.
26. Gardner RA, Kinkade R, Wang C, Phanstiel O (2004) Total synthesis of petrobactin and its homologues as potential growth stimuli for Marinobacter hydrocarbonoclasticus, an oil-degrading bacteria. J Org Chem 69:3530-3537.
27. Harris WR, Amin SA, Kupper FC, Green DH, Carrano CJ (2007) Borate binding to siderophores: Structure and stability. J Am Chem Soc 129:12263-12271.
28. Hickford SJ, et al. (2004) Petrobactin sulfonate, a new siderophore produced by the marine bacterium Marinobacter hydrocarbonoclasticus. J Nat Prod 67:1897-1899.
29. Stols L, et al. (2002) A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site. Protein Expression Purif 25:8-15.
30. Aslanidis C, de Jong PJ (1990) Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res 18:6069-6074.
31. VanDuyne GD, Standaert RF, Karplus PA, Schreiber SL, Clardy J (1993) Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J Mol Biol 229:105-124.
32. Walsh MA, Dementieva I, Evans G, Sanishvili R, Joachimiak A (1999) Taking MAD to the extreme: Ultrafast protein structure determination. Acta Crystallogr D 55:1168-1173.
33. Kim Y, et al. (2004) Automation of protein purification for structural genomics. J Struct Funct Genomics 5:111-118.
34. Minor W, Cymborowski M, Otwinowski Z, Chruszcz M (2006) HKL-3000: The integration of data reduction and structure solution - From diffraction images to an initial model in minutes. Acta Crystallogr D 62:859-866.
35. Sheldrick GM (2008) A short history of SHELX. Acta Crystallogr A 64:112-122.
36. Terwilliger TC (2003) Automated main-chain model building by template matching and iterative fragment extension. Acta Crystallogr D 59:38-44.
37. Otwinowski Z (1991) Daresbury Study Weekend Proceedings, eds Wolf W, Evans PR, Leshe AGW (SERC Daresbury Laboratory, Warrington, UK), pp 80-85.
38. Cowtan KKC (1994) An automated procedure for phase improvement by density modification. Joint CCP4 ESF-EACBM Newslett Protein Crystallogr 31:34-38.
39. Collaborative Computational Project, Number 4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D 50:760-763.
40. Morris RJ, Perrakis A, Lamzin VS (2003) ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol 374:229-244.
41. Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 53:240-255.
42. Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D 60:2126-2132.
43. Laskowski RA, MacArthur MW, Moss DS, Thornton JM (1993) PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Crystallogr 26:283-291.