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InterPro: IPR003815 S-ribosylhomocysteinase (LuxS)

Protein matchesHelp
UniProtKB
Matches:
879 proteins
AccessionHelp IPR003815 S-ribosylhomocysteinase
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR011249 Metalloenzyme, LuxS/M16 peptidase-like, metal-binding
GO Term annotationHelp
Process GO:0009372 quorum sensing
Function GO:0005506 iron ion binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

In bacteria, the regulation of gene expression in response to changes in cell density is called quorum sensing. Quorum-sensing bacteria produce, release, and respond to hormone-like molecules (autoinducers) that accumulate in the external environment as the cell population grows. For example, enteric bacteria use quorum sensing to regulate several traits that allow them to establish and maintain infection in their host, including motility, biofilm formation, and virulence-specific genes [1]. The LuxS/AI-2 system is one of several quorum sensing mechanisms. AI-2 (autoinducer-2) is a signalling molecule that functions in interspecies communication by regulating niche-specific genes with diverse functions in various bacteria, often in response to population density. LuxS (S-ribosylhomocysteinase; EC:4.4.1.21) is an autoinducer-production protein that has a metabolic function as a component of the activated methyl cycle. LuxS converts S-ribosylhomocysteine to homocysteine and 4,5-dihydroxy-2,3-pentanedione (DPD); DPD can then spontaneously cyclise to active AI-2 [2, 3]. LuxS is a homodimeric iron-dependent metalloenzyme containing two identical tetrahedral metal-binding sites similar to those found in peptidases and amidases [4].

Structural linksHelp
SCOP: d.185.1.2
CATH: 3.30.1360.80
Database linksHelp
Enzyme: EC:4.4.1.21
PANDIT: PF02664
Blocks: IPB003815
Pfam Clan: CL0094.8

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR003815 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O34667 S-ribosylhomocysteine lyase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR011249 Metalloenzyme, LuxS/M16 peptidase-like, metal-binding
IPR003815 S-ribosylhomocysteinase (LuxS)
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp
1. Kendall MM, Sperandio V.
Quorum sensing by enteric pathogens.
Curr. Opin. Gastroenterol. 23 10-5 2007 [PubMed: 17133078]
http://dx.doi.org/10.1097/MOG.0b013e3280118289
2. van Houdt R, Moons P, Jansen A, Vanoirbeek K, Michiels CW.
Isolation and functional analysis of luxS in Serratia plymuthica RVH1.
FEMS Microbiol. Lett. 262 201-9 2006 [PubMed: 16923076]
3. Zhu J, Patel R, Pei D.
Catalytic mechanism of S-ribosylhomocysteinase (LuxS): stereochemical course and kinetic isotope effect of proton transfer reactions.
Biochemistry 43 10166-72 2004 [PubMed: 15287744]
http://dx.doi.org/10.1021/bi0491088
4. Rajan R, Zhu J, Hu X, Pei D, Bell CE.
Crystal structure of S-ribosylhomocysteinase (LuxS) in complex with a catalytic 2-ketone intermediate.
Biochemistry 44 3745-53 2005 [PubMed: 15751951]
http://dx.doi.org/10.1021/bi0477384

Additional ReadingHelp
Zhu J, Hu X, Dizin E, Pei D.
Catalytic mechanism of S-ribosylhomocysteinase (LuxS): direct observation of ketone intermediates by 13C NMR spectroscopy.
J. Am. Chem. Soc. 125 2003 13379-81 [PubMed: 14583032]
http://dx.doi.org/10.1021/ja0369663
Bassler BL.
How bacteria talk to each other: regulation of gene expression by quorum sensing.
Curr. Opin. Microbiol. 2 1999 582-7 [PubMed: 10607620]
http://dx.doi.org/10.1016/S1369-5274(99)00025-9
Zhu J, Dizin E, Hu X, Wavreille AS, Park J, Pei D.
S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein.
Biochemistry 42 2003 4717-26 [PubMed: 12705835]
http://dx.doi.org/10.1021/bi034289j
Surette MG, Miller MB, Bassler BL.
Quorum sensing in Escherichia coli, Salmonella typhimurium, and Vibrio harveyi: a new family of genes responsible for autoinducer production.
Proc. Natl. Acad. Sci. U.S.A. 96 1999 1639-44 [PubMed: 9990077]
http://dx.doi.org/10.1073/pnas.96.4.1639
Lewis HA, Furlong EB, Laubert B, Eroshkina GA, Batiyenko Y, Adams JM, Bergseid MG, Marsh CD, Peat TS, Sanderson WE, Sauder JM, Buchanan SG.
A structural genomics approach to the study of quorum sensing: crystal structures of three LuxS orthologs.
Structure 9 2001 527-37 [PubMed: 11435117]
http://dx.doi.org/10.1016/S0969-2126(01)00613-X
Hilgers MT, Ludwig ML.
Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site.
Proc. Natl. Acad. Sci. U.S.A. 98 2001 11169-74 [PubMed: 11553770]
http://dx.doi.org/10.1073/pnas.191223098
Day WA Jr, Maurelli AT.
Shigella flexneri LuxS quorum-sensing system modulates virB expression but is not essential for virulence.
Infect. Immun. 69 2001 15-23 [PubMed: 11119484]
http://dx.doi.org/10.1128/IAI.69.1.15-23.2001
Badger J, Sauder JM, Adams JM, Antonysamy S, Bain K, Bergseid MG, Buchanan SG, Buchanan MD, Batiyenko Y, Christopher JA, Emtage S, Eroshkina A, Feil I, Furlong EB, Gajiwala KS, Gao X, He D, Hendle J, Huber A, Hoda K, Kearins P, Kissinger C, Laubert B, Lewis HA, Lin J, Loomis K, Lorimer D, Louie G, Maletic M, Marsh CD, Miller I, Molinari J, Muller-Dieckmann HJ, Newman JM, Noland BW, Pagarigan B, Park F, Peat TS, Post KW, Radojicic S, Ramos A, Romero R, Rutter ME, Sanderson WE, Schwinn KD, Tresser J, Winhoven J, Wright TA, Wu L, Xu J, Harris TJ.
Structural analysis of a set of proteins resulting from a bacterial genomics project.
Proteins 60 2005 787-96 [PubMed: 16021622]
http://dx.doi.org/10.1002/prot.20541
Shen G, Rajan R, Zhu J, Bell CE, Pei D.
Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase.
J. Med. Chem. 49 2006 3003-11 [PubMed: 16686542]
http://dx.doi.org/10.1021/jm060047g
Joyce EA, Bassler BL, Wright A.
Evidence for a signaling system in Helicobacter pylori: detection of a luxS-encoded autoinducer.
J. Bacteriol. 182 2000 3638-43 [PubMed: 10850976]
http://dx.doi.org/10.1128/JB.182.13.3638-3643.2000
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InterPro 23.1