This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


5t7j

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:37, 6 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='5t7j' size='340' side='right'caption='[[5t7j]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='5t7j' size='340' side='right'caption='[[5t7j]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5t7j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspor Aspor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T7J OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5T7J FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5t7j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_oryzae_RIB40 Aspergillus oryzae RIB40]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T7J FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.65&#8491;</td></tr>
-
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AO090701000246 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=510516 ASPOR])</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=5t7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t7j OCA], [https://pdbe.org/5t7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t7j RCSB], [https://www.ebi.ac.uk/pdbsum/5t7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t7j ProSAT]</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=5t7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t7j OCA], [http://pdbe.org/5t7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t7j RCSB], [http://www.ebi.ac.uk/pdbsum/5t7j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t7j ProSAT]</span></td></tr>
+
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/AA13_ASPOR AA13_ASPOR] Lytic polysaccharide monooxygenase-related protein that has no activity towards starch.<ref>PMID:25608804</ref>
-
Lytic polysaccharide monooxygenases (LPMOs) are a class of copper-dependent enzymes discovered within the last ten years. They oxidatively cleave polysaccharides (chitin, lignocellulose, hemicellulose and starch-derived), presumably making recalcitrant substrates accessible to glycoside hydrolases. Recently, the first crystal structure of an LPMO-substrate complex was reported, giving insights into the interaction of LPMOs with beta-linked substrates (Frandsen et al., 2016). The LPMOs acting on alpha-linked glycosidic bonds (family AA13) display binding surfaces that are quite different from those of LPMOs that act on beta-linked glycosidic bonds (families AA9-AA11), as revealed from the first determined structure (Lo Leggio et al., 2015), and thus presumably the AA13s interact with their substrate in a distinct fashion. Here, several new structures of the same AA13 enzyme, Aspergillus oryzae AA13, are presented. Crystals obtained in the presence of high zinc-ion concentrations were used, as they can be obtained more reproducibly than those used to refine the deposited copper-containing structure. One structure with an ordered zinc-bound active site was solved at 1.65 A resolution, and three structures from crystals soaked with maltooligosaccharides in solutions devoid of zinc ions were solved at resolutions of up to 1.10 A. Despite similar unit-cell parameters, small rearrangements in the crystal packing occur when the crystals are depleted of zinc ions, resulting in a more occluded substrate-binding surface. In two of the three structures maltooligosaccharide ligands are bound, but not at the active site. Two of the structures presented show a His-ligand conformation that is incompatible with metal-ion binding. In one of these structures this conformation is the principal one (80% occupancy), giving a rare atomic resolution view of a substantially misfolded enzyme that is presumably rendered inactive.
+
-
Learning from oligosaccharide soaks of crystals of an AA13 lytic polysaccharide monooxygenase: crystal packing, ligand binding and active-site disorder.,Frandsen KE, Poulsen JC, Tovborg M, Johansen KS, Lo Leggio L Acta Crystallogr D Struct Biol. 2017 Jan 1;73(Pt 1):64-76. doi:, 10.1107/S2059798316019641. Epub 2017 Jan 1. PMID:28045386<ref>PMID:28045386</ref>
+
==See Also==
-
 
+
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5t7j" style="background-color:#fffaf0;"></div>
+
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Aspor]]
+
[[Category: Aspergillus oryzae RIB40]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Frandsen, K E.H]]
+
[[Category: Frandsen KEH]]
-
[[Category: Johansen, K S]]
+
[[Category: Johansen KS]]
-
[[Category: Leggio, L Lo]]
+
[[Category: Lo Leggio L]]
-
[[Category: Poulsen, J C.N]]
+
[[Category: Poulsen J-CN]]
-
[[Category: Tovborg, M]]
+
[[Category: Tovborg M]]
-
[[Category: Aspergillus oryzae aa13 lpmo]]
+
-
[[Category: Enzyme]]
+
-
[[Category: Metal binding protein]]
+

Current revision

X-ray crystal structure of AA13 LPMO

PDB ID 5t7j

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools