6jqb: Difference between revisions
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<StructureSection load='6jqb' size='340' side='right'caption='[[6jqb]], [[Resolution|resolution]] 1.10Å' scene=''> | <StructureSection load='6jqb' size='340' side='right'caption='[[6jqb]], [[Resolution|resolution]] 1.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6jqb]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6jqb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pelomonas_saccharophila Pelomonas saccharophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JQB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JQB FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.101Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7SA:ACARBOSE+DERIVED+HEPTASACCHARIDE'>7SA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=6jqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jqb OCA], [https://pdbe.org/6jqb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jqb RCSB], [https://www.ebi.ac.uk/pdbsum/6jqb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jqb ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/AMT4_ROSSA AMT4_ROSSA] | |||
<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: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pelomonas saccharophila]] | ||
[[Category: | [[Category: Ban XF]] | ||
[[Category: | [[Category: Gu ZB]] | ||
[[Category: | [[Category: Jin TC]] | ||
[[Category: Li | [[Category: Li CM]] | ||
[[Category: Li | [[Category: Li YL]] | ||
[[Category: | [[Category: Li ZF]] | ||
[[Category: | [[Category: Shang YH]] | ||
[[Category: | [[Category: Zhang ZQ]] | ||
Latest revision as of 12:04, 9 October 2024
The structure of maltooligosaccharide-forming amylase from Pseudomonas saccharophila STB07 with pseudo-maltoheptaoseThe structure of maltooligosaccharide-forming amylase from Pseudomonas saccharophila STB07 with pseudo-maltoheptaose
Structural highlights
FunctionPublication Abstract from PubMedThe maltooligosaccharide-forming amylases (MFAses) degrade starch into maltooligosaccharides which potentially benefit human diet and grow popular in food processing, but little has been studied about their product specificity and structures. We focused on this topic and provide evidence through an X-ray crystal structure of the maltotetraose (G4)-forming amylase from Pseudomonas saccharophila STB07 (MFAps), as well as co-crystal structures of MFAps with G4 and with pseudo-maltoheptaose (pseudo-G7) determined at up to 1.1 A resolution. G4 and pseudo-G7 occupy active cleft subsites -4 to -1 and -4 to +3 respectively. Binding induces conformational changes in the active sites except Asp193, working as the base catalyst. Comparison of the MFAps structure with those of other alpha-amylases revealed obvious differences in the loop structures providing dominant interactions between protein and substrate in the non-reducing side of the active sites cleft. These structures at the non-reducing end may govern the G4 specificity of MFAps and also be relevant to its exo-type action pattern. Structure of maltotetraose-forming amylase from Pseudomonas saccharophila STB07 provides insights into its product specificity.,Zhang Z, Jin T, Xie X, Ban X, Li C, Hong Y, Cheng L, Gu Z, Li Z Int J Biol Macromol. 2019 Nov 18. pii: S0141-8130(19)37071-0. doi:, 10.1016/j.ijbiomac.2019.11.006. PMID:31751711[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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