4mck
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Crystal structure of Family GH19, Class IV chitinase from Zea mays== | |
| - | + | <StructureSection load='4mck' size='340' side='right' caption='[[4mck]], [[Resolution|resolution]] 1.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4mck]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Maize Maize]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MCK OCA]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mcl|4mcl]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">chiA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4577 MAIZE])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mck OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mck RCSB], [http://www.ebi.ac.uk/pdbsum/4mck PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Maize ChitA chitinase is composed of a small, hevein-like domain attached to a carboxy-terminal chitinase domain. During fungal ear rot, the hevein-like domain is cleaved by secreted fungal proteases to produce truncated forms of ChitA. Here, we report a structural and biochemical characterization of truncated ChitA (ChitA DeltaN), which lacks the hevein-like domain. ChitA DeltaN and a mutant form (ChitA DeltaN-EQ) were expressed and purified; enzyme assays showed that ChitA DeltaN activity was comparable to the full-length enzyme. Mutation of Glu62 to Gln (ChitA DeltaN-EQ) abolished chitinase activity without disrupting substrate binding, demonstrating that Glu62 is directly involved in catalysis. A crystal structure of ChitA DeltaN-EQ provided strong support for key roles for Glu62, Arg177, and Glu165 in hydrolysis, and for Ser103 and Tyr106 in substrate binding. These findings demonstrate that the hevein-like domain is not needed for enzyme activity. Moreover, comparison of the crystal structure of this plant class IV chitinase with structures from larger class I and II enzymes suggest that class IV chitinases have evolved to accommodate shorter substrates. | ||
| - | + | Crystallographic structure of ChitA, a glycoside hydrolase family 19, plant class IV chitinase from Zea mays.,Chaudet MM, Naumann TA, Price NP, Rose DR Protein Sci. 2014 Feb 6. doi: 10.1002/pro.2437. PMID:24616181<ref>PMID:24616181</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Chitinase]] | [[Category: Chitinase]] | ||
| + | [[Category: Maize]] | ||
[[Category: Chaudet, M M.]] | [[Category: Chaudet, M M.]] | ||
[[Category: Rose, D R.]] | [[Category: Rose, D R.]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 06:46, 7 May 2014
Crystal structure of Family GH19, Class IV chitinase from Zea mays
| |||||||||||
Categories: Chitinase | Maize | Chaudet, M M. | Rose, D R. | Hydrolase
