View source for 5hop


==1.65 Angstrom resolution crystal structure of lmo0182 (residues 1-245) from Listeria monocytogenes EGD-e==
<StructureSection load='5hop' size='340' side='right'caption='[[5hop]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hop]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HOP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HOP 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]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5hop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hop OCA], [https://pdbe.org/5hop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hop RCSB], [https://www.ebi.ac.uk/pdbsum/5hop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hop ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8YAE8_LISMO Q8YAE8_LISMO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Active in the aqueous cellular environment where a massive excess of water is perpetually present, enzymes that catalyze the transfer of an electrophile to a non-water nucleophile (transferases) require specific strategies to inhibit mechanistically related hydrolysis reactions. To identify principles that confer transferase versus hydrolase reaction specificity, we exploited two enzymes that use highly similar catalytic apparatuses to catalyze the transglycosylation (a transferase reaction) or hydrolysis of alpha-1,3-glucan linkages in the cyclic tetrasaccharide cycloalternan (CA). We show that substrate binding to non-catalytic domains and a conformationally stable active site promote CA transglycosylation, whereas a distinct pattern of active site conformational change is associated with CA hydrolysis. These findings defy the classic view of induced-fit conformational change and illustrate a mechanism by which a stable hydrophobic binding site can favor transferase activity and disfavor hydrolysis. Application of these principles could facilitate the rational reengineering of transferases with desired catalytic properties.

Transferase Versus Hydrolase: The Role of Conformational Flexibility in Reaction Specificity.,Light SH, Cahoon LA, Mahasenan KV, Lee M, Boggess B, Halavaty AS, Mobashery S, Freitag NE, Anderson WF Structure. 2017 Jan 5. pii: S0969-2126(16)30397-5. doi:, 10.1016/j.str.2016.12.007. PMID:28089449<ref>PMID:28089449</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hop" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Listeria monocytogenes EGD-e]]
[[Category: Anderson WF]]
[[Category: Grimshaw S]]
[[Category: Halavaty AS]]
[[Category: Kwon K]]
[[Category: Light SH]]
[[Category: Minasov G]]