3fhq: Difference between revisions

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-{{Seed}}
-[[Image:3fhq.jpg|left|200px]]
-<!--
+==Structure of endo-beta-N-acetylglucosaminidase A==
-The line below this paragraph, containing "STRUCTURE_3fhq", creates the "Structure Box" on the page.
+<StructureSection load='3fhq' size='340' side='right'caption='[[3fhq]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3fhq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Glutamicibacter_protophormiae Glutamicibacter protophormiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FHQ FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.452&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NGT:3AR,5R,6S,7R,7AR-5-HYDROXYMETHYL-2-METHYL-5,6,7,7A-TETRAHYDRO-3AH-PYRANO[3,2-D]THIAZOLE-6,7-DIOL'>NGT</scene></td></tr>
-{{STRUCTURE_3fhq|  PDB=3fhq  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fhq OCA], [https://pdbe.org/3fhq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fhq RCSB], [https://www.ebi.ac.uk/pdbsum/3fhq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fhq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9ZB22_9MICC Q9ZB22_9MICC]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/3fhq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3fhq ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Endo-beta-N-acetylglucosaminidases (ENGases) are dual specificity enzymes with an ability to catalyze hydrolysis and transglycosylation reactions. Recently, these enzymes have become the focus of intense research because of their potential for synthesis of glycopeptides. We have determined the 3D structures of an ENGase from Arthrobacter protophormiae (Endo-A) in 3 forms, one in native form, one in complex with Man(3)GlcNAc-thiazoline and another in complex with GlcNAc-Asn. The carbohydrate moiety sits above the TIM-barrel in a cleft region surrounded by aromatic residues. The conserved essential catalytic residues - E173, N171 and Y205 are within hydrogen bonding distance of the substrate. W216 and W244 regulate access to the active site during transglycosylation by serving as "gate-keepers". Interestingly, Y299F mutation resulted in a 3 fold increase in the transglycosylation activity. The structure provides insights into the catalytic mechanism of GH85 family of glycoside hydrolases at molecular level and could assist rational engineering of ENGases.
-===Structure of endo-beta-N-acetylglucosaminidase A===
+Structural basis and catalytic mechanism for the dual functional endo-beta-N-acetylglucosaminidase A.,Yin J, Li L, Shaw N, Li Y, Song JK, Zhang W, Xia C, Zhang R, Joachimiak A, Zhang HC, Wang LX, Liu ZJ, Wang P PLoS ONE. 2009;4(3):e4658. Epub 2009 Mar 2. PMID:19252736<ref>PMID:19252736</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_19252736}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3fhq" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 19252736 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19252736}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Glutamicibacter protophormiae]]
-FHQ is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Arthrobacter_protophormiae Arthrobacter protophormiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FHQ OCA].
+[[Category: Large Structures]]
+[[Category: Jie Y]]
-==Reference==
+[[Category: Joachimiak A]]
-<ref group="xtra">PMID:19252736</ref><references group="xtra"/>
+[[Category: Li L]]
-[[Category: Arthrobacter protophormiae]]
+[[Category: Li Y]]
-[[Category: Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase]]
+[[Category: Liu Z-J]]
-[[Category: Jie, Y.]]
+[[Category: Shaw N]]
-[[Category: Joachimiak, A.]]
+[[Category: Song J]]
-[[Category: Li, L.]]
+[[Category: Wang L-X]]
-[[Category: Li, Y.]]
+[[Category: Wang P]]
-[[Category: Liu, Z J.]]
+[[Category: Xia C]]
-[[Category: Shaw, N.]]
+[[Category: Zhang H-C]]
-[[Category: Song, J.]]
+[[Category: Zhang R]]
-[[Category: Wang, L X.]]
+[[Category: Zhang W]]
-[[Category: Wang, P.]]
-[[Category: Xia, C.]]
-[[Category: Zhang, H C.]]
-[[Category: Zhang, R.]]
-[[Category: Zhang, W.]]
-[[Category: Endo-a]]
-[[Category: Glcnac-asn]]
-[[Category: Glycoprotein]]
-[[Category: Glycosidase]]
-[[Category: Hydrolase]]
-[[Category: Man3glcnac-thiazoline]]
-[[Category: X-ray structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May  6 09:59:43 2009''