1ifv
From Proteopedia
(New page: 200px<br /><applet load="1ifv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ifv, resolution 2.25Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1ifv.jpg|left|200px]]<br /><applet load="1ifv" size=" | + | [[Image:1ifv.jpg|left|200px]]<br /><applet load="1ifv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ifv, resolution 2.25Å" /> | caption="1ifv, resolution 2.25Å" /> | ||
'''CRYSTAL STRUCTURE OF PATHOGENESIS-RELATED PROTEIN LLPR10.1B FROM YELLOW LUPINE'''<br /> | '''CRYSTAL STRUCTURE OF PATHOGENESIS-RELATED PROTEIN LLPR10.1B FROM YELLOW LUPINE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Pathogenesis-related class 10 (PR10) proteins are restricted to the plant | + | Pathogenesis-related class 10 (PR10) proteins are restricted to the plant kingdom where they are coded by multigene families and occur at high levels. In spite of their abundance, their physiological role is obscure although members of a distantly related subclass (cytokinin-specific binding proteins) are known to bind plant hormones. PR10 proteins are of special significance in legume plants where their expression patterns are related to infection by the symbiotic, nitrogen-fixing bacteria. Here we present the first crystal structures of classic PR10 proteins representing two homologues from one subclass in yellow lupine. The general fold is similar and, as in a birch pollen allergen, consists of a seven-stranded beta-sheet wrapped around a long C-terminal helix. The mouth of a large pocket formed between the beta-sheet and the helix seems a likely site for ligand binding. The shape of the pocket varies because, in variance with the rigid beta-sheet, the helix shows unusual conformational variability consisting in bending, disorder, and axial shifting. A surface loop, proximal to the entrance to the internal cavity, shows an unusual structural conservation and rigidity in contrast to the high glycine content in its sequence. The loop is different from the so-called glycine-rich P-loops that bind phosphate groups of nucleotides, but it is very likely that it does play a role in ligand binding in PR10 proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 1IFV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lupinus_luteus Lupinus luteus]. Full crystallographic information is available from [http:// | + | 1IFV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lupinus_luteus Lupinus luteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IFV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bujacz, G.]] | [[Category: Bujacz, G.]] | ||
[[Category: Jaskolski, M.]] | [[Category: Jaskolski, M.]] | ||
| - | [[Category: Sikorski, M | + | [[Category: Sikorski, M M.]] |
[[Category: 7-stranded beta sheet]] | [[Category: 7-stranded beta sheet]] | ||
[[Category: c-terminal helix]] | [[Category: c-terminal helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:25 2008'' |
Revision as of 11:11, 21 February 2008
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CRYSTAL STRUCTURE OF PATHOGENESIS-RELATED PROTEIN LLPR10.1B FROM YELLOW LUPINE
Overview
Pathogenesis-related class 10 (PR10) proteins are restricted to the plant kingdom where they are coded by multigene families and occur at high levels. In spite of their abundance, their physiological role is obscure although members of a distantly related subclass (cytokinin-specific binding proteins) are known to bind plant hormones. PR10 proteins are of special significance in legume plants where their expression patterns are related to infection by the symbiotic, nitrogen-fixing bacteria. Here we present the first crystal structures of classic PR10 proteins representing two homologues from one subclass in yellow lupine. The general fold is similar and, as in a birch pollen allergen, consists of a seven-stranded beta-sheet wrapped around a long C-terminal helix. The mouth of a large pocket formed between the beta-sheet and the helix seems a likely site for ligand binding. The shape of the pocket varies because, in variance with the rigid beta-sheet, the helix shows unusual conformational variability consisting in bending, disorder, and axial shifting. A surface loop, proximal to the entrance to the internal cavity, shows an unusual structural conservation and rigidity in contrast to the high glycine content in its sequence. The loop is different from the so-called glycine-rich P-loops that bind phosphate groups of nucleotides, but it is very likely that it does play a role in ligand binding in PR10 proteins.
About this Structure
1IFV is a Single protein structure of sequence from Lupinus luteus. Full crystallographic information is available from OCA.
Reference
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
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