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| - | [[Image:1agy.gif|left|200px]] | |
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| - | <!-- | + | ==The 1.15 angstrom refined structure of fusarium solani pisi cutinase== |
| - | The line below this paragraph, containing "STRUCTURE_1agy", creates the "Structure Box" on the page.
| + | <StructureSection load='1agy' size='340' side='right'caption='[[1agy]], [[Resolution|resolution]] 1.15Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[1agy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_vanettenii Fusarium vanettenii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AGY FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15Å</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=1agy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1agy OCA], [https://pdbe.org/1agy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1agy RCSB], [https://www.ebi.ac.uk/pdbsum/1agy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1agy ProSAT]</span></td></tr> |
| - | {{STRUCTURE_1agy| PDB=1agy | SCENE= }}
| + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CUTI1_FUSVN CUTI1_FUSVN] Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:18658138, PubMed:8286366, PubMed:8555209, PubMed:19810726). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:18658138, PubMed:8286366, PubMed:8555209, PubMed:19810726). Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of fungal infection (Ref.4).<ref>PMID:18658138</ref> <ref>PMID:19810726</ref> <ref>PMID:8286366</ref> <ref>PMID:8555209</ref> [PROSITE-ProRule:PRU10109] |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ag/1agy_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1agy ConSurf]. |
| | + | <div style="clear:both"></div> |
| | | | |
| - | '''THE 1.15 ANGSTROM REFINED STRUCTURE OF FUSARIUM SOLANI PISI CUTINASE'''
| + | ==See Also== |
| - | | + | *[[Cutinase 3D structures|Cutinase 3D structures]] |
| - | | + | == References == |
| - | ==Overview==
| + | <references/> |
| - | X-ray data have been recorded to 1.0 A resolution from a crystal of Fusarium solani cutinase using synchrotron radiation and an imaging-plate scanner. The anisotropic treatment of thermal motion led to a fivefold increase in accuracy and to a considerable quality improvement in the electron density maps with respect to an intermediate isotropic model. The final model has an R-factor of 9.4%, with a mean coordinate error of 0.021 A, as estimated from inversion of the least-squares matrix. The availability of an accurate structure at atomic resolution and of meaningful estimates of the errors in its atomic parameters, allowed an extensive analysis of several stereochemical parameters, such as peptide planarity, main-chain and some side-chain bond distances. The hydrogen atoms could be clearly identified in the electron density, thus providing unambiguous evidence on the protonation state of the catalytic histidine residue. The atomic resolution revealed an appreciable extent of flexibility in the cutinase active site, which might be correlated with a possible adaptation to different substrates. The anisotropic treatment of thermal factors provided insights into the anisotropic nature of motions. The analysis of these motions in the two loops delimiting the catalytic crevice pointed out a "breath-like" movement in the substrate binding region of cutinase.
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==About this Structure== | + | [[Category: Fusarium vanettenii]] |
| - | 1AGY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_solani_subsp._pisi Fusarium solani subsp. pisi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AGY OCA].
| + | [[Category: Large Structures]] |
| - | | + | [[Category: Cambillau C]] |
| - | ==Reference== | + | [[Category: Martinez C]] |
| - | Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis., Longhi S, Czjzek M, Lamzin V, Nicolas A, Cambillau C, J Mol Biol. 1997 May 16;268(4):779-99. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9175860 9175860]
| + | [[Category: Nicolas A]] |
| - | [[Category: Fusarium solani subsp. pisi]] | + | |
| - | [[Category: Single protein]] | + | |
| - | [[Category: Cambillau, C.]] | + | |
| - | [[Category: Martinez, C.]] | + | |
| - | [[Category: Nicolas, A.]] | + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Serine esterase]]
| + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:15:20 2008''
| + | |
| Structural highlights
Function
CUTI1_FUSVN Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:18658138, PubMed:8286366, PubMed:8555209, PubMed:19810726). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:18658138, PubMed:8286366, PubMed:8555209, PubMed:19810726). Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of fungal infection (Ref.4).[1] [2] [3] [4] [PROSITE-ProRule:PRU10109]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Chen S, Tong X, Woodard RW, Du G, Wu J, Chen J. Identification and characterization of bacterial cutinase. J Biol Chem. 2008 Sep 19;283(38):25854-62. PMID:18658138 doi:10.1074/jbc.M800848200
- ↑ Liu Z, Gosser Y, Baker PJ, Ravee Y, Lu Z, Alemu G, Li H, Butterfoss GL, Kong XP, Gross R, Montclare JK. Structural and functional studies of Aspergillus oryzae cutinase: enhanced thermostability and hydrolytic activity of synthetic ester and polyester degradation. J Am Chem Soc. 2009 Nov 4;131(43):15711-6. PMID:19810726 doi:10.1021/ja9046697
- ↑ Martinez C, Nicolas A, van Tilbeurgh H, Egloff MP, Cudrey C, Verger R, Cambillau C. Cutinase, a lipolytic enzyme with a preformed oxyanion hole. Biochemistry. 1994 Jan 11;33(1):83-9. PMID:8286366
- ↑ Nicolas A, Egmond M, Verrips CT, de Vlieg J, Longhi S, Cambillau C, Martinez C. Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state. Biochemistry. 1996 Jan 16;35(2):398-410. PMID:8555209 doi:http://dx.doi.org/10.1021/bi9515578
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