View source for 3ngm


==Crystal structure of lipase from Gibberella zeae==
<StructureSection load='3ngm' size='340' side='right'caption='[[3ngm]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ngm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_graminearum Fusarium graminearum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NGM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=3ngm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ngm OCA], [https://pdbe.org/3ngm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ngm RCSB], [https://www.ebi.ac.uk/pdbsum/3ngm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ngm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6WER3_GIBZA Q6WER3_GIBZA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fusarium graminearum (sexual stage: Gibberella zeae) is the causative agent of Fusarium Head Blight (FHB), which is one of the most destructive plant disease of cereals, accounting for high grain yield losses, especially for wheat and maize. Like other fungal pathogens, several extracellular enzymes secreted by G. zeae are known to be involved in host infection. Among these secreted lipases, G. zeae lipase (GZEL), which is encoded by the FGL1 gene, was demonstrated to be crucial to G. zeae pathogenicity. However, the precise mechanism of GZEL remains unclear due to a lack of detailed structural information. In this study, we report the crystal structure of GZEL at the atomic level. The structure of GZEL displays distinct structural differences compared to reported homologues and indicates a unique "double lock" enzymatic mechanism. To gain insight into substrate/inhibitor recognition, we proposed a model of GZEL in complex with substrate and the lipase inhibitor ebelactone B (based on the reported structures of GZEL homologues), which defines possible substrate binding sites within the catalytic cleft and suggests an "anti sn-l" binding mode. These results pave the way to elucidating the mechanism of GZEL and thus provide clues for the design of anti-FHB inhibitors.

Crystal structure of a secreted lipase from Gibberella zeae reveals a novel "double-lock" mechanism.,Lou Z, Li M, Sun Y, Liu Y, Liu Z, Wu W, Rao Z Protein Cell. 2010 Aug;1(8):760-70. Epub 2010 Aug 28. PMID:21203917<ref>PMID:21203917</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ngm" style="background-color:#fffaf0;"></div>

==See Also==
*[[Lipase 3D Structures|Lipase 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Fusarium graminearum]]
[[Category: Large Structures]]
[[Category: Li M]]
[[Category: Liu Y]]
[[Category: Liu Z]]
[[Category: Lou ZY]]
[[Category: Rao ZH]]
[[Category: Sun YN]]