About: The Three-Dimensional Structure of Pectate Lyase E, a Plant Virulence Factor from Erwinia chrysanthemi

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About: The Three-Dimensional Structure of Pectate Lyase E, a Plant Virulence Factor from Erwinia chrysanthemi Goto Sponge NotDistinct Permalink

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scientific article published on 01 November 1994

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в листопаді 1994 (uk) im November 1994 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en payares de 1994 (ast) scientific article published on 01 November 1994 (en)
publication date	wds:Q74790190-CDE5A097-F7B2-4424-95E4-7333D55D3A38
publication date	1994-11-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q74790190-9397071E-2173-4354-8331-C52992031890
language of work or name	English
cites work	wds:Q74790190-090955DC-FCA6-4175-B6B8-CC82CA76DF1B wds:Q74790190-39229ADD-7137-4981-8BA6-5F44316C6856 wds:Q74790190-40FAD947-F3C7-4AB2-8615-A98F6658A13A wds:Q74790190-514BBC11-74C3-49AC-A437-4B7F2806077C wds:Q74790190-599D4C39-60F1-49C9-A4F1-5586E88A79B0 wds:Q74790190-5FBDAB2B-0EAA-47E3-8FAA-CAE2102CE791 wds:Q74790190-69F03E54-4204-4BD9-8932-C847D1DF7D59 wds:Q74790190-8610D400-96C0-4A1D-9869-4C4D1596BFD3 wds:Q74790190-8A2FE14B-1A98-4441-BD41-AD23D4DB0C5D wds:Q74790190-95E4739B-4B33-467D-9B18-C77EE98FC6D0 wds:Q74790190-B4FCCD84-4D76-44EB-988E-8617328397FB wds:Q74790190-BF3D595C-7599-4C8F-B056-63F090DCCD82 wds:Q74790190-C3ADA4AD-1453-4867-987B-04C13DE9C302 wds:Q74790190-CBF52DEC-F714-40EE-B224-6C1B6D4559D7 wds:Q74790190-D5098A6B-EBD4-4667-88E9-C07D82A0A834 wds:Q74790190-D83C0FFA-88B3-4B81-9115-67EB95F1560F wds:Q74790190-DA655B1D-47CB-47EB-AFB9-E3B490EB521F wds:Q74790190-E39A9F5E-92D3-4CD5-8467-F8798EB8D45F wds:Q74790190-EB71B736-0444-42F4-8E3B-1695887BCB8B wds:Q74790190-F020E485-8A5D-4E74-91D9-76DD05BCADC1 wds:Q74790190-F5170D85-4DEE-44BC-A3E3-CB3EAB707864 wds:Q74790190-FD801B96-FE69-4C28-85E0-2597FCF07620
cites work	Stereochemical quality of protein structure coordinates Aromatic-aromatic interaction: a mechanism of protein structure stabilization Hydrogen bonding in globular proteins Beta-turns and their distortions: a proposed new nomenclature. Unusual structural features in the parallel beta-helix in pectate lyases Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO Structure and organization of the pel genes from Erwinia chrysanthemi EC16. Structure of two pectate lyase genes from Erwinia chrysanthemi EC16 and their high-level expression in Escherichia coli. Extracellular and periplasmic isoenzymes of pectate lyase from Erwinia carotovora subspecies carotovora belong to different gene families. Cloned Erwinia chrysanthemi out genes enable Escherichia coli to selectively secrete a diverse family of heterologous proteins to its milieu Cloning of Amb a I (antigen E), the major allergen family of short ragweed pollen Differential depolymerization mechanisms of pectate lyases secreted by Erwinia chrysanthemi EC16 Preliminary crystallographic analysis of a plant pathogenic factor: pectate lyase Conformations and interactions of pectins Crystallographic R factor refinement by molecular dynamics Assessment of protein models with three-dimensional profiles Loops in globular proteins: a novel category of secondary structure The parallel beta helix of pectate lyase C: something to sneeze at. Analysis of eight out genes in a cluster required for pectic enzyme secretion by Erwinia chrysanthemi: sequence comparison with secretion genes from other gram-negative bacteria Some of the out genes involved in the secretion of pectate lyases in Erwinia chrysanthemi are regulated by kdgR Pectate lyase from Fusarium solani f. sp. pisi: purification, characterization, in vitro translation of the mRNA, and involvement in pathogenicity
author name string	wds:Q74790190-274708DD-B027-4377-8449-1D1DAA08B3E5 wds:Q74790190-8117BA18-F748-4492-AC8F-E4A0A32FAF85 wds:Q74790190-AC92AA82-319F-4B0B-8B9D-8BD84590357D wds:Q74790190-FD043EEB-B711-41FB-A6CD-8A6A324BE031
author name string	F. Jurnak M. D. Yoder S. E. Lietzke N. T. Keen
rdfs:label	The Three-Dimensional Structure of Pectate Lyase E, a Plant Virulence Factor from Erwinia chrysanthemi (en) The Three-Dimensional Structure of Pectate Lyase E, a Plant Virulence Factor from Erwinia chrysanthemi (nl)
skos:prefLabel	The Three-Dimensional Structure of Pectate Lyase E, a Plant Virulence Factor from Erwinia chrysanthemi (en) The Three-Dimensional Structure of Pectate Lyase E, a Plant Virulence Factor from Erwinia chrysanthemi (nl)
name	The Three-Dimensional Structure of Pectate Lyase E, a Plant Virulence Factor from Erwinia chrysanthemi (en) The Three-Dimensional Structure of Pectate Lyase E, a Plant Virulence Factor from Erwinia chrysanthemi (nl)
title	wds:Q74790190-7A61333A-95BF-482F-B6C4-A4A53869FFF8
title	The Three-Dimensional Structure of Pectate Lyase E, a Plant Virulence Factor from Erwinia chrysanthemi (en)
page(s)	wds:Q74790190-4536E4BC-A770-4A3E-903B-E0CEB543DE36
page(s)	849-862
instance of	wds:Q74790190-8D3FE0A0-241A-469F-AE7D-DB57F6F31101
instance of	scholarly article
main subject	wds:Q74790190-F9071D64-C4BB-4C60-87E7-F3796D4B3E6D
main subject	Erwinia chrysanthemi
PubMed ID	wds:Q74790190-0309AE1A-6828-4C19-AF14-CC984868EAE3
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12232373
PubMed ID	12232373
published in	wds:Q74790190-287A66BA-6F4A-46D5-8126-14BEA0F2EA4F
published in	Plant Physiology
issue	wds:Q74790190-B76DA63E-4D40-4C84-BA53-F7779B3B206B
volume	wds:Q74790190-596DB86A-F8C2-4C7E-9C84-85650E1DC93A
issue	3
volume	106
number of pages	wds:Q74790190-7102F6A1-C20A-4323-A5EE-A740D32B19C9
number of pages	14 (xsd:decimal)
DOI	wds:Q74790190-44DBFC4A-3157-49E0-8C01-C7B3227538BE
DOI	http://dx.doi.org/10.1104/PP.106.3.849
DOI	10.1104/PP.106.3.849
PMCID	wds:Q74790190-72ADBB66-C569-4CAB-9789-03AF1CBC6395
PMCID	159608
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q74790190
is cites work of	The interdigitated beta-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilization Identification of amino acid residues critical for catalysis and stability in Aspergillus niger family 1 pectin lyase A. Structure and function of pectic enzymes: virulence factors of plant pathogens Structural biology of pectin degradation by Enterobacteriaceae A left-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila The architecture of parallel beta-helices and related folds Characterization and functional expression of a ubiquitously expressed tomato pectin methylesterase.

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