4j0l: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4j0l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Secale_cereale Secale cereale]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J0L FirstGlance]. <br>
<table><tr><td colspan='2'>[[4j0l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Secale_cereale Secale cereale]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J0L FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4j0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j0l OCA], [https://pdbe.org/4j0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j0l RCSB], [https://www.ebi.ac.uk/pdbsum/4j0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j0l ProSAT]</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=4j0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j0l OCA], [https://pdbe.org/4j0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j0l RCSB], [https://www.ebi.ac.uk/pdbsum/4j0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j0l ProSAT]</span></td></tr>
</table>
</table>

Latest revision as of 17:18, 8 November 2023

Crystal Structure of a Family GH19 Chitinase (W72A/E67Q mutant) from rye seeds in complex with two (GlcNAc)4 moleculesCrystal Structure of a Family GH19 Chitinase (W72A/E67Q mutant) from rye seeds in complex with two (GlcNAc)4 molecules

Structural highlights

4j0l is a 1 chain structure with sequence from Secale cereale. 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

CHIC_SECCE Defense against chitin containing fungal pathogens. Binds the hyphal tips of fungi and degrades nascent chitin.[1] [2] [3]

Publication Abstract from PubMed

Crystallographic analysis of a mutated form of "loopful" GH19 chitinase from rye seeds a double mutant RSC-c, in which Glu67 and Trp72 are mutated to glutamine and alanine, respectively, (RSC-c-E67Q/W72A) in complex with chitin tetrasaccharide (GlcNAc)(4) revealed that the entire substrate-binding cleft was completely occupied with the sugar residues of two (GlcNAc)(4) molecules. One (GlcNAc)(4) molecule bound to subsites -4 to -1, while the other bound to subsites +1 to +4. Comparisons of the main chain conformation between liganded RSC-c-E67Q/W72A and unliganded wild type RSC-c suggested domain motion essential for catalysis. This is the first report on the complete subsite mapping of GH19 chitinase.

Complete subsite mapping of a "loopful" GH19 chitinase from rye seeds based on its crystal structure.,Ohnuma T, Umemoto N, Kondo K, Numata T, Fukamizo T FEBS Lett. 2013 Aug 19;587(16):2691-7. doi: 10.1016/j.febslet.2013.07.008. Epub, 2013 Jul 18. PMID:23871710[4]

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

See Also

References

  1. ↑ Ohnuma T, Yagi M, Yamagami T, Taira T, Aso Y, Ishiguro M. Molecular cloning, functional expression, and mutagenesis of cDNA encoding rye (Secale cereale) seed chitinase-c. Biosci Biotechnol Biochem. 2002 Feb;66(2):277-84. PMID:11999399
  2. ↑ Taira T, Yamagami T, Aso Y, Ishiguro M, Ishihara M. Localization, accumulation, and antifungal activity of chitinases in rye (Secale cereale) seed. Biosci Biotechnol Biochem. 2001 Dec;65(12):2710-8. PMID:11826968
  3. ↑ Taira T, Ohnuma T, Yamagami T, Aso Y, Ishiguro M, Ishihara M. Antifungal activity of rye (Secale cereale) seed chitinases: the different binding manner of class I and class II chitinases to the fungal cell walls. Biosci Biotechnol Biochem. 2002 May;66(5):970-7. PMID:12092848
  4. ↑ Ohnuma T, Umemoto N, Kondo K, Numata T, Fukamizo T. Complete subsite mapping of a "loopful" GH19 chitinase from rye seeds based on its crystal structure. FEBS Lett. 2013 Aug 19;587(16):2691-7. doi: 10.1016/j.febslet.2013.07.008. Epub, 2013 Jul 18. PMID:23871710 doi:http://dx.doi.org/10.1016/j.febslet.2013.07.008

4j0l, resolution 1.90Å

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