3r4z

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Current revision (08:35, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3r4z' size='340' side='right'caption='[[3r4z]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
<StructureSection load='3r4z' size='340' side='right'caption='[[3r4z]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3r4z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Microbulbifer_degradans_2-40 Microbulbifer degradans 2-40]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R4Z FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3r4z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharophagus_degradans_2-40 Saccharophagus degradans 2-40]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R4Z FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3r4y|3r4y]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Sde_2657 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=203122 Microbulbifer degradans 2-40])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3r4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r4z OCA], [https://pdbe.org/3r4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r4z RCSB], [https://www.ebi.ac.uk/pdbsum/3r4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r4z ProSAT]</span></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=3r4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r4z OCA], [https://pdbe.org/3r4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r4z RCSB], [https://www.ebi.ac.uk/pdbsum/3r4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r4z ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q21HB2_SACD2 Q21HB2_SACD2]
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In agarolytic microorganisms, alpha-neoagarobiose hydrolase (NABH) is an essential enzyme to metabolize agar because it converts alpha-neoagarobiose (O-3,6-anhydro-alpha-l-galactopyranosyl-(1,3)-d-galactose) into fermentable monosaccharides (d-galactose and 3,6-anhydro-l-galactose) in the agarolytic pathway. NABH can be divided into two biological classes by its cellular location. Here, we describe a structure and function of cytosolic NABH from Saccharophagus degradans 2-40 in a native protein and d-galactose complex determined at 2.0 and 1.55 A, respectively. The overall fold is organized in an N-terminal helical extension and a C-terminal five-bladed beta-propeller catalytic domain. The structure of the enzyme-ligand (d-galactose) complex predicts a +1 subsite in the substrate binding pocket. The structural features may provide insights for the evolution and classification of NABH in agarolytic pathways.
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Crystal structure of a key enzyme in the agarolytic pathway, alpha-neoagarobiose hydrolase from Saccharophagus degradans 2-40.,Ha SC, Lee S, Lee J, Kim HT, Ko HJ, Kim KH, Choi IG Biochem Biophys Res Commun. 2011 Aug 26;412(2):238-44. Epub 2011 Jul 23. PMID:21810409<ref>PMID:21810409</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3r4z" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Microbulbifer degradans 2-40]]
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[[Category: Saccharophagus degradans 2-40]]
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[[Category: Bang, W G]]
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[[Category: Bang WG]]
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[[Category: Choi, I G]]
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[[Category: Choi IG]]
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[[Category: Ha, S C]]
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[[Category: Ha SC]]
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[[Category: Kim, K H]]
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[[Category: Kim KH]]
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[[Category: Kim, S H]]
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[[Category: Kim SH]]
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[[Category: Lee, J Y]]
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[[Category: Lee JY]]
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[[Category: Lee, S]]
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[[Category: Lee S]]
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[[Category: Shin, D H]]
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[[Category: Shin DH]]
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[[Category: 6-anhydro-l-galactose]]
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[[Category: Agar metabolism]]
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[[Category: Alpha-d-galactopyranose]]
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[[Category: Bioenergy]]
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[[Category: Hydrolase]]
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[[Category: Neoagarobiose]]
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Current revision

Crystal structure of alpha-neoagarobiose hydrolase (ALPHA-NABH) in complex with alpha-d-galactopyranose from Saccharophagus degradans 2-40

PDB ID 3r4z

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