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2a3b

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Current revision

Crystal structure of Aspergillus fumigatus chitinase B1 in complex with caffeine

Structural highlights

2a3b is a 2 chain structure with sequence from Aspergillus fumigatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Family 18 chitinases play key roles in a range of pathogenic organisms and are overexpressed in the asthmatic lung. By screening a library of marketed drug molecules, we have identified methylxanthine derivatives as possible inhibitor leads. These derivatives, theophylline, caffeine, and pentoxifylline, are used therapeutically as antiinflammatory agents, with pleiotropic mechanisms of action. Here it is shown that they are also competitive inhibitors against a fungal family 18 chitinase, with pentoxifylline being the most potent (K(i) of 37 microM). Crystallographic analysis of chitinase-inhibitor complexes revealed specific interactions with the active site, mimicking the reaction intermediate analog, allosamidin. Mutagenesis identified the key active site residues, conserved in mammalian chitinases, which contribute to inhibitor affinity. Enzyme assays also revealed that these methylxanthines are active against human chitinases.

Methylxanthine drugs are chitinase inhibitors: investigation of inhibition and binding modes.,Rao FV, Andersen OA, Vora KA, Demartino JA, van Aalten DM Chem Biol. 2005 Sep;12(9):973-80. PMID:16183021^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rao FV, Andersen OA, Vora KA, Demartino JA, van Aalten DM. Methylxanthine drugs are chitinase inhibitors: investigation of inhibition and binding modes. Chem Biol. 2005 Sep;12(9):973-80. PMID:16183021 doi:10.1016/j.chembiol.2005.07.009

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2a3b"

@@ Line 3: / Line 3: @@
 <StructureSection load='2a3b' size='340' side='right'caption='[[2a3b]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2a3b]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A3B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A3B FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2a3b]] 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=2A3B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A3B FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CFF:CAFFEINE'>CFF</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.9&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w9p|1w9p]], [[1w9v|1w9v]], [[1w9u|1w9u]], [[2a3a|2a3a]], [[2a3c|2a3c]], [[2a3e|2a3e]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CFF:CAFFEINE'>CFF</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2a3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a3b OCA], [https://pdbe.org/2a3b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a3b RCSB], [https://www.ebi.ac.uk/pdbsum/2a3b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a3b 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=2a3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a3b OCA], [http://pdbe.org/2a3b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a3b RCSB], [http://www.ebi.ac.uk/pdbsum/2a3b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2a3b ProSAT]</span></td></tr>
 </table>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Chitinase]]
+[[Category: Aspergillus fumigatus]]
 [[Category: Large Structures]]
-[[Category: Aalten, D M.F van]]
+[[Category: Andersen OA]]
-[[Category: Andersen, O A]]
+[[Category: DeMartino JA]]
-[[Category: DeMartino, J A]]
+[[Category: Rao FV]]
-[[Category: Rao, F V]]
+[[Category: Vora KA]]
-[[Category: Vora, K A]]
+[[Category: Van Aalten DMF]]
-[[Category: Chitinase-caffeine complex]]
-[[Category: Hydrolase]]

2a3b

From Proteopedia

Current revision

Crystal structure of Aspergillus fumigatus chitinase B1 in complex with caffeine

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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