1xdf

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{{STRUCTURE_1xdf| PDB=1xdf | SCENE= }}
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'''Crystal structure of pathogenesis-related protein LlPR-10.2A from yellow lupine'''
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===Crystal structure of pathogenesis-related protein LlPR-10.2A from yellow lupine===
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==Overview==
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Pathogenesis-related (PR) proteins of class 10 are abundant in higher plants. Some of these proteins are induced under stress conditions as part of the plant defence mechanism. Other homologues are developmentally regulated and their expression varies in different plant organs. The PR-10 proteins are encoded by multigene families, have a weight of about 17 kDa and are found in the cytosol. In yellow lupin, nine different homologues have been identified and divided into two subclasses, LlPR-10.1 and LlPR-10.2. Within each subclass the sequence identity is about 75-91%, while across the subclasses it is only 59-60%. Here, the crystal structure of a yellow lupin PR-10 protein from the second subclass, LlPR-10.2A, is presented. The structure was solved by molecular replacement and refined to R = 0.205 using 1.9 A resolution data. The general fold of LlPR-10.2A resembles that of the other PR-10 proteins and consists of a long C-terminal alpha-helix surrounded by a seven-stranded antiparallel beta-sheet, with two shorter alpha-helices located between strands beta1 and beta2. The most variable part of the structure, the C-terminal helix, is strongly kinked towards the beta-sheet core in both LlPR-10.2A molecules present in the asymmetric unit. This unexpected feature reduces the size of the hydrophobic cavity observed in other PR-10 proteins that is reported to be the ligand-binding site. As in other PR-10 structures, a surface loop located near the entrance to the cavity shows very high structural conservation and stability despite the high glycine content in its sequence.
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{{ABSTRACT_PUBMED_15608381}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structure of a yellow lupin pathogenesis-related PR-10 protein belonging to a novel subclass., Pasternak O, Biesiadka J, Dolot R, Handschuh L, Bujacz G, Sikorski MM, Jaskolski M, Acta Crystallogr D Biol Crystallogr. 2005 Jan;61(Pt 1):99-107. Epub 2004, Dec 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15608381 15608381]
Structure of a yellow lupin pathogenesis-related PR-10 protein belonging to a novel subclass., Pasternak O, Biesiadka J, Dolot R, Handschuh L, Bujacz G, Sikorski MM, Jaskolski M, Acta Crystallogr D Biol Crystallogr. 2005 Jan;61(Pt 1):99-107. Epub 2004, Dec 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15608381 15608381]
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Crystal structures of two homologous pathogenesis-related proteins from yellow lupine., Biesiadka J, Bujacz G, Sikorski MM, Jaskolski M, J Mol Biol. 2002 Jun 21;319(5):1223-34. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12079359 12079359]
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Crystallization and preliminary x-ray structure determination of Lupinus luteus PR10 protein., Biesiadka J, Sikorski MM, Bujacz G, Jaskolski M, Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1925-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10531497 10531497]
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X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy., Gajhede M, Osmark P, Poulsen FM, Ipsen H, Larsen JN, Joost van Neerven RJ, Schou C, Lowenstein H, Spangfort MD, Nat Struct Biol. 1996 Dec;3(12):1040-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8946858 8946858]
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Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier., Markovic-Housley Z, Degano M, Lamba D, von Roepenack-Lahaye E, Clemens S, Susani M, Ferreira F, Scheiner O, Breiteneder H, J Mol Biol. 2003 Jan 3;325(1):123-33. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12473456 12473456]
[[Category: Lupinus luteus]]
[[Category: Lupinus luteus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Glycine-rich loop]]
[[Category: Glycine-rich loop]]
[[Category: Kinked c-terminal alpha-helix]]
[[Category: Kinked c-terminal alpha-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:22:55 2008''

Revision as of 04:22, 28 July 2008

Image:1xdf.png

Template:STRUCTURE 1xdf

Crystal structure of pathogenesis-related protein LlPR-10.2A from yellow lupine

Template:ABSTRACT PUBMED 15608381

About this Structure

1XDF is a Single protein structure of sequence from Lupinus luteus. Full crystallographic information is available from OCA.

Reference

Structure of a yellow lupin pathogenesis-related PR-10 protein belonging to a novel subclass., Pasternak O, Biesiadka J, Dolot R, Handschuh L, Bujacz G, Sikorski MM, Jaskolski M, Acta Crystallogr D Biol Crystallogr. 2005 Jan;61(Pt 1):99-107. Epub 2004, Dec 17. PMID:15608381

Crystal structures of two homologous pathogenesis-related proteins from yellow lupine., Biesiadka J, Bujacz G, Sikorski MM, Jaskolski M, J Mol Biol. 2002 Jun 21;319(5):1223-34. PMID:12079359

Crystallization and preliminary x-ray structure determination of Lupinus luteus PR10 protein., Biesiadka J, Sikorski MM, Bujacz G, Jaskolski M, Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1925-7. PMID:10531497

X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy., Gajhede M, Osmark P, Poulsen FM, Ipsen H, Larsen JN, Joost van Neerven RJ, Schou C, Lowenstein H, Spangfort MD, Nat Struct Biol. 1996 Dec;3(12):1040-5. PMID:8946858

Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier., Markovic-Housley Z, Degano M, Lamba D, von Roepenack-Lahaye E, Clemens S, Susani M, Ferreira F, Scheiner O, Breiteneder H, J Mol Biol. 2003 Jan 3;325(1):123-33. PMID:12473456

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