doi: 10.1126/science.8502994.
New domain motif: the structure of pectate lyase C, a secreted plant virulence factor
Affiliations
- PMID: 8502994
- DOI: 10.1126/science.8502994
Item in Clipboard
New domain motif: the structure of pectate lyase C, a secreted plant virulence factor
Science.
.
Abstract
Pectate lyases are secreted by pathogens and initiate soft-rot diseases in plants by cleaving polygalacturonate, a major component of the plant cell wall. The three-dimensional structure of pectate lyase C from Erwinia chrysanthemi has been solved and refined to a resolution of 2.2 angstroms. The enzyme folds into a unique motif of parallel beta strands coiled into a large helix. Within the core, the amino acids form linear stacks and include a novel asparagine ladder. The sequence similarities that pectate lyases share with pectin lyases, pollen and style proteins, and tubulins suggest that the parallel beta helix motif may occur in a broad spectrum of proteins.
Similar articles
-
Structure of a plant cell wall fragment complexed to pectate lyase C.Plant Cell. 1999 Jun;11(6):1081-92. doi: 10.1105/tpc.11.6.1081. Plant Cell. 1999. PMID: 10368179 Free PMC article.
-
Characterization of the pelL gene encoding a novel pectate lyase of Erwinia chrysanthemi 3937.Mol Microbiol. 1995 Jun;16(6):1183-95. doi: 10.1111/j.1365-2958.1995.tb02341.x. Mol Microbiol. 1995. PMID: 8577252
-
Structure-based multiple alignment of extracellular pectate lyase sequences.Mol Plant Microbe Interact. 1995 Mar-Apr;8(2):331-4. doi: 10.1094/mpmi-8-0331. Mol Plant Microbe Interact. 1995. PMID: 7756698
-
On a (beta-) roll.Trends Biochem Sci. 1993 Sep;18(9):313-4. doi: 10.1016/0968-0004(93)90061-q. Trends Biochem Sci. 1993. PMID: 8236448 Review. No abstract available.
-
Structure and evolution of parallel beta-helix proteins.J Struct Biol. 1998;122(1-2):236-46. doi: 10.1006/jsbi.1998.3985. J Struct Biol. 1998. PMID: 9724625 Review.
Cited by
-
Expression and Characterization of Hyperthermostable Exo-polygalacturonase TtGH28 from Thermotoga thermophilus.Mol Biotechnol. 2016 Jul;58(7):509-19. doi: 10.1007/s12033-016-9948-8. Mol Biotechnol. 2016. PMID: 27209035
-
Characterization of two potentially universal turn motifs that shape the repeated five-residues fold--crystal structure of a lumenal pentapeptide repeat protein from Cyanothece 51142.Protein Sci. 2006 Nov;15(11):2579-95. doi: 10.1110/ps.062407506. Protein Sci. 2006. PMID: 17075135 Free PMC article.
-
Polysaccharide lyase: molecular cloning, sequencing, and overexpression of the xanthan lyase gene of Bacillus sp. strain GL1.Appl Environ Microbiol. 2001 Feb;67(2):713-20. doi: 10.1128/AEM.67.2.713-720.2001. Appl Environ Microbiol. 2001. PMID: 11157235 Free PMC article.
-
Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates.FASEB J. 1996 Jan;10(1):57-66. doi: 10.1096/fasebj.10.1.8566549. FASEB J. 1996. PMID: 8566549 Free PMC article. Review.
-
Structure of a plant cell wall fragment complexed to pectate lyase C.Plant Cell. 1999 Jun;11(6):1081-92. doi: 10.1105/tpc.11.6.1081. Plant Cell. 1999. PMID: 10368179 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
