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| | ==Crystal structure of Aspergillus fumigatus chitinase B1 in complex with monopeptide== | | ==Crystal structure of Aspergillus fumigatus chitinase B1 in complex with monopeptide== |
| - | <StructureSection load='3chc' size='340' side='right' caption='[[3chc]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='3chc' size='340' side='right'caption='[[3chc]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3chc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CHC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CHC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3chc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CHC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZRG:(2S)-2-ACETAMIDO-N-METHYL-5-[[N-(METHYLCARBAMOYL)CARBAMIMIDOYL]AMINO]PENTANAMIDE'>ZRG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w9v|1w9v]], [[1w9p|1w9p]], [[3ch9|3ch9]], [[3chd|3chd]], [[3che|3che]], [[3chf|3chf]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZRG:(2S)-2-ACETAMIDO-N-METHYL-5-[[N-(METHYLCARBAMOYL)CARBAMIMIDOYL]AMINO]PENTANAMIDE'>ZRG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] </span></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=3chc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3chc OCA], [https://pdbe.org/3chc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3chc RCSB], [https://www.ebi.ac.uk/pdbsum/3chc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3chc ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3chc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3chc OCA], [http://pdbe.org/3chc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3chc RCSB], [http://www.ebi.ac.uk/pdbsum/3chc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3chc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CHIB1_ASPFM CHIB1_ASPFM]] Major secreted chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Plays a role in the morphogenesis and autolysis (By similarity). | + | [https://www.uniprot.org/uniprot/CHIB1_ASPFM CHIB1_ASPFM] Major secreted chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Plays a role in the morphogenesis and autolysis (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Chitinase|Chitinase]] | + | *[[Chitinase 3D structures|Chitinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chitinase]] | + | [[Category: Aspergillus fumigatus]] |
| - | [[Category: Aalten, D M.F van]] | + | [[Category: Large Structures]] |
| - | [[Category: Andersen, O A]] | + | [[Category: Andersen OA]] |
| - | [[Category: Glycosidase]] | + | [[Category: Van Aalten DMF]] |
| - | [[Category: Hydrolase]]
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| - | [[Category: Hydrolase-hydrolase inhibitor complex]]
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| - | [[Category: Peptide inhibitor]]
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| Structural highlights
Function
CHIB1_ASPFM Major secreted chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Plays a role in the morphogenesis and autolysis (By similarity).
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
Chitinase inhibitors have chemotherapeutic potential as fungicides, pesticides, and antiasthmatics. Argifin, a natural product cyclopentapeptide, competitively inhibits family 18 chitinases in the nanomolar to micromolar range and shows extensive substrate mimicry. In an attempt to map the active fragments of this large natural product, the cyclopentapeptide was progressively dissected down to four linear peptides and dimethylguanylurea, synthesized using a combination of solution and solid phase peptide synthesis. The peptide fragments inhibit chitinase B1 from Aspergillus fumigatus (AfChiB1), the human chitotriosidase, and chitinase activity in lung homogenates from a murine model of chronic asthma, with potencies ranging from high nanomolar to high micromolar inhibition. X-ray crystallographic analysis of the chitinase-inhibitor complexes revealed that the conformations of the linear peptides were remarkably similar to that of the natural product. Strikingly, the dimethylguanylurea fragment, representing only a quarter of the natural product mass, was found to harbor all significant interactions with the protein and binds with unusually high efficiency. The data provide useful information that could lead to the generation of drug-like, natural product-based chitinase inhibitors.
Structure-based dissection of the natural product cyclopentapeptide chitinase inhibitor argifin.,Andersen OA, Nathubhai A, Dixon MJ, Eggleston IM, van Aalten DM Chem Biol. 2008 Mar;15(3):295-301. PMID:18355729[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Andersen OA, Nathubhai A, Dixon MJ, Eggleston IM, van Aalten DM. Structure-based dissection of the natural product cyclopentapeptide chitinase inhibitor argifin. Chem Biol. 2008 Mar;15(3):295-301. PMID:18355729 doi:10.1016/j.chembiol.2008.02.015
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