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| [[Image:1afp.jpg|left|200px]]<br /><applet load="1afp" size="450" color="white" frame="true" align="right" spinBox="true"
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| '''SOLUTION STRUCTURE OF THE ANTIFUNGAL PROTEIN FROM ASPERGILLUS GIGANTEUS. EVIDENCE FOR DISULPHIDE CONFIGURATIONAL ISOMERISM'''<br />
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| ==Overview== | | ==SOLUTION STRUCTURE OF THE ANTIFUNGAL PROTEIN FROM ASPERGILLUS GIGANTEUS. EVIDENCE FOR DISULPHIDE CONFIGURATIONAL ISOMERISM== |
| The solution structure of the antifungal protein (AFP, 51 residues, 4, disulfide bridges) from Aspergillus giganteus has been determined by using, experimentally derived interproton distance constraints from nuclear, magnetic resonance (NMR) spectroscopy. Complete sequence-specific proton, assignments were obtained at pH 5.0 and 35 degrees C. A set of 834 upper, limit distance constraints from nuclear Overhauser effect measurements was, used as input for the calculation of structures with the program DIANA. An, initial family of 40 structures calculated with no disulfide constraints, was used to obtain information about the disulfide connectivities, which, could not be determined by standard biochemical methods. Three possible, disulfide patterns were selected and the corresponding disulfide, constraints applied to generate a family of 20 DIANA conformers for each, pattern. Following energy minimization, the average pairwise RMSD of the, 20 conformers of each family is 1.01, 0.89, and 1.01 A for backbone atoms, and 1.82, 1.74, and 1.81 A for all heavy atoms. One of these three, families contains the disulfide bridge arrangement actually present in the, solution structure of AFP. Although the three families fulfill the NMR, constraints, one of the disulfide patterns considered (cysteine pairs, 7-33, 14-40, 26-49, 28-51) is favored among the others on the basis of, previous chemical studies. It thus probably corresponds to the actual, pattern of disulfide bridges present in the protein, and the corresponding, family represents the solution structure of AFP. The folding of AFP, consists of five antiparallel beta strands connected in a -1, -1, +3, +1, topology and highly twisted, defining a small and compact beta barrel, stabilized by four internal disulfide bridges. A cationic site formed by, up to three lysine side chains adjacent to a hydrophobic stretch, both at, the protein surface, may constitute a potential binding site for, phospholipids which would be the basis of its biological function. On the, other hand, a second, minor form of AFP has been detected. NMR data, together with results from mass spectrometry, chemical analysis, and, sedimentation equilibrium, suggest that this species differs from the, major form in the pairs of cysteines involved in the four disulfide, bridges.
| | <StructureSection load='1afp' size='340' side='right'caption='[[1afp]]' scene=''> |
| | | == Structural highlights == |
| ==About this Structure== | | <table><tr><td colspan='2'>[[1afp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_giganteus Aspergillus giganteus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AFP FirstGlance]. <br> |
| 1AFP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_giganteus Aspergillus giganteus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AFP OCA].
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1afp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1afp OCA], [https://pdbe.org/1afp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1afp RCSB], [https://www.ebi.ac.uk/pdbsum/1afp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1afp ProSAT]</span></td></tr> |
| ==Reference== | | </table> |
| NMR solution structure of the antifungal protein from Aspergillus giganteus: evidence for cysteine pairing isomerism., Campos-Olivas R, Bruix M, Santoro J, Lacadena J, Martinez del Pozo A, Gavilanes JG, Rico M, Biochemistry. 1995 Mar 7;34(9):3009-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7893713 7893713]
| | == Function == |
| | [https://www.uniprot.org/uniprot/AFP_ASPGI AFP_ASPGI] This protein inhibits the growth of a variety of fungal species. |
| | __TOC__ |
| | </StructureSection> |
| [[Category: Aspergillus giganteus]] | | [[Category: Aspergillus giganteus]] |
| [[Category: Single protein]] | | [[Category: Large Structures]] |
| [[Category: Bruix, M.]] | | [[Category: Bruix M]] |
| [[Category: Campos-Olivas, R.]] | | [[Category: Campos-Olivas R]] |
| [[Category: Gavilanes, J.G.]] | | [[Category: Del Pozo AM]] |
| [[Category: Lacadena, J.]] | | [[Category: Gavilanes JG]] |
| [[Category: Pozo, A.M.Del.]] | | [[Category: Lacadena J]] |
| [[Category: Rico, M.]] | | [[Category: Rico M]] |
| [[Category: Santoro, J.]] | | [[Category: Santoro J]] |
| [[Category: antifungal protein]]
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| ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:49:06 2007''
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