1r76
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(New page: 200px<br /><applet load="1r76" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r76, resolution 2.65Å" /> '''Structure of a pecta...)
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Revision as of 20:09, 24 November 2007
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Structure of a pectate lyase from Azospirillum irakense
Overview
The three-dimensional structure of Azospirillum irakense pectate lyase, (PelA) has been determined at a resolution of 2.65 A. The crystals are, hexagonal, belonging to space group P6(5)22, with unit-cell parameters a =, b = 85.37, c = 231.32 angstroms. Phase information was derived from a, multiple-wavelength anomalous dispersion (MAD) experiment using a Hg, derivative. Refinement of the model converged to Rcryst = 20.08% and Rfree, = 25.87%. The overall structure of PelA does not adopt the characteristic, parallel beta-helix fold displayed by pectate lyases from polysaccharide, lyase (PL) families PL1, PL3 and PL9. Instead, it displays a predominantly, alpha-helical structure with irregular coils and short beta-strands, similar to the recently reported structure of the catalytic module of the, Cellvibrio japonicus pectate lyase Pel10Acm. The topologies of the two, structures have been compared. They show two 'domains' with the interface, between them being a wide-open central groove in which the active site is, located. The active sites of the crystal structures are also compared and, their similarities and differences are discussed.
About this Structure
1R76 is a Single protein structure of sequence from Azospirillum irakense with HG, CL, IPA and GOL as ligands. Active as Pectate lyase, with EC number 4.2.2.2 Full crystallographic information is available from OCA.
Reference
Azospirillum irakense pectate lyase displays a toroidal fold., Novoa De Armas H, Verboven C, De Ranter C, Desair J, Vande Broek A, Vanderleyden J, Rabijns A, Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):999-1007. Epub 2004, May 21. PMID:15159558
Page seeded by OCA on Sat Nov 24 22:16:31 2007
