1bxm | pdb_00001bxm

ENGINEERED BETA-CRYPTOGEIN COMPLEXED WITH ERGOSTEROL

spinqualitylabelsall models 1bxm, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1bxm is a 1 chain structure with sequence from Halophytophthora cryptogea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ERG Gene: CRY (MUTATED LYS 13 HIS) (Halophytophthora cryptogea) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ELIB_PHYCR] Induces local and distal defense responses (incompatible hypersensitive reaction) in plants from the solanaceae and cruciferae families. Elicits leaf necrosis and causes the accumulation of pathogenesis-related proteins. Might interact with the lipidic molecules of the plasma membrane. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Elicitins, produced by most of the phytopathogenic fungi of the genus Phytophthora, provoke in tobacco both remote leaf necrosis and the induction of a resistance against subsequent attack by various microorganisms. Despite the recent description of the three-dimensional crystal structure of cryptogein (CRY), the molecular basis of the interactions between Phytophthora and plants largely remains unknown. The X-ray crystal structure, refined at 2.1 A, of a ligand complexed, mutated CRY, K13H, is reported. Analysis of this structure reveals that CRY is able to encapsulate a ligand that induces only a minor conformational change in the protein structure. The ligand has been identified as an ergosterol by gas chromatographic analysis coupled with mass spectrometry analysis. This result is consistent with biochemical data that have shown that elicitins are a distinct class of Sterol Carrier Proteins (SCP). Data presented here provide the first structural description of the pertinent features of the elicitin sterol interaction and permit a reassessment of the importance of both the key residue 13 and the mobility of the omega loop for the accessibility of the sterol to the cavity. The biological implications thereof are discussed. This paper reports the first structure of a SCP/sterol complex. The 2.1 A structure of an elicitin-ergosterol complex: a recent addition to the Sterol Carrier Protein family.,Boissy G, O'Donohue M, Gaudemer O, Perez V, Pernollet JC, Brunie S Protein Sci. 1999 Jun;8(6):1191-9. PMID:10386869 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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