1chk

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Current revision (06:43, 7 February 2024) (edit) (undo)
 
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<StructureSection load='1chk' size='340' side='right'caption='[[1chk]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1chk' size='340' side='right'caption='[[1chk]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1chk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CHK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1chk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._N174 Streptomyces sp. N174]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CHK FirstGlance]. <br>
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</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=1chk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1chk OCA], [https://pdbe.org/1chk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1chk RCSB], [https://www.ebi.ac.uk/pdbsum/1chk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1chk ProSAT]</span></td></tr>
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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]] 2.4&#8491;</td></tr>
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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=1chk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1chk OCA], [https://pdbe.org/1chk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1chk RCSB], [https://www.ebi.ac.uk/pdbsum/1chk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1chk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CHIS_STRSN CHIS_STRSN]] Aids in the defense against invading fungal pathogens by degrading their cell wall chitosan.
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[https://www.uniprot.org/uniprot/CHIS_STRSN CHIS_STRSN] Aids in the defense against invading fungal pathogens by degrading their cell wall chitosan.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1chk ConSurf].
</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=1chk ConSurf].
<div style="clear:both"></div>
<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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We report the 2.4 A X-ray crystal structure of a protein with chitosan endo-hydrolase activity isolated from Streptomyces N174. The structure was solved using phases acquired by SIRAS from a two-site methyl mercury derivative combined with solvent flattening and non-crystallographic two-fold symmetry averaging, and refined to an R-factor of 18.5%. The mostly alpha-helical fold reveals a structural core shared with several classes of lysozyme and barley endochitinase, in spite of a lack of shared sequence. Based on this structural similarity we postulate a putative active site, mechanism of action and mode of substrate recognition. It appears that Glu 22 acts as an acid and Asp 40 serves as a general base to activate a water molecule for an SN2 attack on the glycosidic bond. A series of amino-acid side chains and backbone carbonyl groups may bind the polycationic chitosan substrate in a deep electronegative binding cleft.
 
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X-ray structure of an anti-fungal chitosanase from streptomyces N174.,Marcotte EM, Monzingo AF, Ernst SR, Brzezinski R, Robertus JD Nat Struct Biol. 1996 Feb;3(2):155-62. PMID:8564542<ref>PMID:8564542</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 1chk" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Marcotte, E M]]
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[[Category: Streptomyces sp. N174]]
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[[Category: Robertus, J D]]
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[[Category: Marcotte EM]]
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[[Category: Anti-fungal protein]]
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[[Category: Robertus JD]]
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[[Category: Hydrolase]]
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[[Category: O-glycosyl]]
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Current revision

STREPTOMYCES N174 CHITOSANASE PH5.5 298K

PDB ID 1chk

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