1w1y

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[[Image:1w1y.gif|left|200px]]
 
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{{Structure
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==Crystal structure of S. marcescens chitinase B in complex with the cyclic dipeptide inhibitor cyclo-(L-Tyr-L-Pro) at 1.85 A resolution==
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|PDB= 1w1y |SIZE=350|CAPTION= <scene name='initialview01'>1w1y</scene>, resolution 1.85&Aring;
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<StructureSection load='1w1y' size='340' side='right'caption='[[1w1y]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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|SITE= <scene name='pdbsite=BC6:Typ+Binding+Site+For+Chain+B'>BC6</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TYP:CYCLO-(L-TYROSINE-L-PROLINE)+INHIBITOR'>TYP</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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<table><tr><td colspan='2'>[[1w1y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W1Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W1Y FirstGlance]. <br>
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|ACTIVITY= [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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TYP:CYCLO-(L-TYROSINE-L-PROLINE)+INHIBITOR'>TYP</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w1y OCA], [https://pdbe.org/1w1y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w1y RCSB], [https://www.ebi.ac.uk/pdbsum/1w1y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w1y ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q54276_SERMA Q54276_SERMA]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w1/1w1y_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1w1y ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Family 18 chitinases play an essential role in a range of pathogens and pests. Several inhibitors are known, including the potent inhibitors argadin and allosamidin, and the structures of these in complex with chitinases have been elucidated. Recent structural analysis has revealed that CI-4 [cyclo-(L-Arg-D-Pro)] inhibits family 18 chitinases by mimicking the structure of the proposed reaction intermediate. Here we report the high-resolution structures of four new CI-4 derivatives, cyclo-(L-Arg-L-Pro), cyclo-(Gly-L-Pro), cyclo-(L-His-L-Pro), and cyclo-(L-Tyr-L-Pro), in complex with a family 18 chitinase. In addition, details of enzyme inhibition and in vivo activity against Saccharomyces cerevisiae are presented. The structures reveal that the common cyclo-(Gly-Pro) substructure is sufficient for binding, allowing modification of the side chain of the nonproline residue. This suggests that design of cyclic dipeptides with a view to increasing inhibition of family 18 chitinases should be possible through relatively accessible chemistry. The derivatives presented here in complex with chitinase B from Serratia marcescens provide further insight into the mechanism of inhibition of chitinases by cyclic dipeptides as well as providing a new scaffold for chitinase inhibitor design.
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'''CRYSTAL STRUCTURE OF S. MARCESCENS CHITINASE B IN COMPLEX WITH THE CYCLIC DIPEPTIDE INHIBITOR CYCLO-(L-TYR-L-PRO) AT 1.85 A RESOLUTION'''
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Structure-based exploration of cyclic dipeptide chitinase inhibitors.,Houston DR, Synstad B, Eijsink VG, Stark MJ, Eggleston IM, van Aalten DM J Med Chem. 2004 Nov 4;47(23):5713-20. PMID:15509170<ref>PMID:15509170</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1w1y" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Family 18 chitinases play an essential role in a range of pathogens and pests. Several inhibitors are known, including the potent inhibitors argadin and allosamidin, and the structures of these in complex with chitinases have been elucidated. Recent structural analysis has revealed that CI-4 [cyclo-(L-Arg-D-Pro)] inhibits family 18 chitinases by mimicking the structure of the proposed reaction intermediate. Here we report the high-resolution structures of four new CI-4 derivatives, cyclo-(L-Arg-L-Pro), cyclo-(Gly-L-Pro), cyclo-(L-His-L-Pro), and cyclo-(L-Tyr-L-Pro), in complex with a family 18 chitinase. In addition, details of enzyme inhibition and in vivo activity against Saccharomyces cerevisiae are presented. The structures reveal that the common cyclo-(Gly-Pro) substructure is sufficient for binding, allowing modification of the side chain of the nonproline residue. This suggests that design of cyclic dipeptides with a view to increasing inhibition of family 18 chitinases should be possible through relatively accessible chemistry. The derivatives presented here in complex with chitinase B from Serratia marcescens provide further insight into the mechanism of inhibition of chitinases by cyclic dipeptides as well as providing a new scaffold for chitinase inhibitor design.
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*[[Chitinase 3D structures|Chitinase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1W1Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W1Y OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Structure-based exploration of cyclic dipeptide chitinase inhibitors., Houston DR, Synstad B, Eijsink VG, Stark MJ, Eggleston IM, van Aalten DM, J Med Chem. 2004 Nov 4;47(23):5713-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15509170 15509170]
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[[Category: Chitinase]]
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[[Category: Serratia marcescens]]
[[Category: Serratia marcescens]]
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[[Category: Single protein]]
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[[Category: Eggleston I]]
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[[Category: Aalten, D M.F Van.]]
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[[Category: Eijsink VGH]]
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[[Category: Eggleston, I.]]
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[[Category: Houston DR]]
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[[Category: Eijsink, V G.H.]]
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[[Category: Synstad B]]
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[[Category: Houston, D R.]]
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[[Category: Van Aalten DMF]]
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[[Category: Synstad, B.]]
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[[Category: GOL]]
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[[Category: SO4]]
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[[Category: TYP]]
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[[Category: chitinase]]
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[[Category: cyclic dipeptide]]
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[[Category: glycoside hydrolase]]
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[[Category: structure-based inhibitor design]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:50:57 2008''
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Current revision

Crystal structure of S. marcescens chitinase B in complex with the cyclic dipeptide inhibitor cyclo-(L-Tyr-L-Pro) at 1.85 A resolution

PDB ID 1w1y

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