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| | <StructureSection load='5hxm' size='340' side='right'caption='[[5hxm]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='5hxm' size='340' side='right'caption='[[5hxm]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hxm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_monocytogenes_hominis"_nyfeldt_1932 "bacterium monocytogenes hominis" nyfeldt 1932]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HXM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HXM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hxm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HXM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.9Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kmq|4kmq]], [[4kwu|4kwu]], [[5hpo|5hpo]]</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=5hxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hxm OCA], [https://pdbe.org/5hxm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hxm RCSB], [https://www.ebi.ac.uk/pdbsum/5hxm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hxm ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yicI_4, ABE87_12155, ARD00_02746 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1639 "Bacterium monocytogenes hominis" Nyfeldt 1932])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-D-xyloside_xylohydrolase Alpha-D-xyloside xylohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.177 3.2.1.177] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5hxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hxm OCA], [http://pdbe.org/5hxm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hxm RCSB], [http://www.ebi.ac.uk/pdbsum/5hxm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hxm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8Y4J2_LISMO Q8Y4J2_LISMO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium monocytogenes hominis nyfeldt 1932]] | |
| - | [[Category: Alpha-D-xyloside xylohydrolase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Anderson, W F]] | + | [[Category: Listeria monocytogenes]] |
| - | [[Category: Structural genomic]] | + | [[Category: Anderson WF]] |
| - | [[Category: Grimshaw, S]] | + | [[Category: Grimshaw S]] |
| - | [[Category: Halavaty, A S]] | + | [[Category: Halavaty AS]] |
| - | [[Category: Light, S H]] | + | [[Category: Light SH]] |
| - | [[Category: Minasov, G]] | + | [[Category: Minasov G]] |
| - | [[Category: Peterson, S]] | + | [[Category: Peterson S]] |
| - | [[Category: Shuvalova, L]] | + | [[Category: Shuvalova L]] |
| - | [[Category: Winsor, J]] | + | [[Category: Winsor J]] |
| - | [[Category: Csgid]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Idp05250]]
| + | |
| - | [[Category: Listeria monocytogenes egd-e]]
| + | |
| - | [[Category: Lmo2446]]
| + | |
| Structural highlights
5hxm is a 1 chain structure with sequence from Listeria monocytogenes. 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
Q8Y4J2_LISMO
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Light SH, Cahoon LA, Mahasenan KV, Lee M, Boggess B, Halavaty AS, Mobashery S, Freitag NE, Anderson WF. Transferase Versus Hydrolase: The Role of Conformational Flexibility in Reaction Specificity. Structure. 2017 Jan 5. pii: S0969-2126(16)30397-5. doi:, 10.1016/j.str.2016.12.007. PMID:28089449 doi:http://dx.doi.org/10.1016/j.str.2016.12.007
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