4cmr: Difference between revisions

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'''Unreleased structure'''


The entry 4cmr is ON HOLD  until sometime in the future
==The crystal structure of novel exo-type maltose-forming amylase(Py04_0872) from Pyrococcus sp. ST04==
<StructureSection load='4cmr' size='340' side='right'caption='[[4cmr]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4cmr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_sp._ST04 Pyrococcus sp. ST04]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CMR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4cmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cmr OCA], [https://pdbe.org/4cmr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cmr RCSB], [https://www.ebi.ac.uk/pdbsum/4cmr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cmr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I3RE04_9EURY I3RE04_9EURY]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A novel maltose-forming alpha-amylase (PSMA) was recently found in the hyperthermophilic archaeon Pyrococcus sp. ST04. This enzyme shows &lt;13% amino-acid sequence identity to other known alpha-amylases and displays a unique enzymatic property in that it hydrolyzes both alpha-1,4-glucosidic and alpha-1,6-glucosidic linkages of substrates, recognizing only maltose units, in an exo-type manner. Here, the crystal structure of PSMA at a resolution of 1.8 A is reported, showing a tight ring-shaped tetramer with monomers composed of two domains: an N-domain (amino acids 1-341) with a typical GH57 family (beta/alpha)7-barrel fold and a C-domain (amino acids 342-597) composed of alpha-helical bundles. A small closed cavity observed in proximity to the catalytic residues Glu153 and Asp253 at the domain interface has the appropriate volume and geometry to bind a maltose unit, accounting for the selective exo-type maltose hydrolysis of the enzyme. A narrow gate at the putative subsite +1 formed by residue Phe218 and Phe452 is essential for specific cleavage of glucosidic bonds. The closed cavity at the active site is connected to a short substrate-binding channel that extends to the central hole of the tetramer, exhibiting a geometry that is significantly different from classical maltogenic amylases or beta-amylases. The structural features of this novel exo-type maltose-forming alpha-amylase provide a molecular basis for its unique enzymatic characteristics and for its potential use in industrial applications and protein engineering.


Authors: Park, K.-H., Jung, J.-H., Park, C.-S., Woo, E.-J.
Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04.,Park KH, Jung JH, Park SG, Lee ME, Holden JF, Park CS, Woo EJ Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1659-68. doi:, 10.1107/S1399004714006567. Epub 2014 May 30. PMID:24914977<ref>PMID:24914977</ref>


Description: The crystal structure of novel exo-type maltose-forming amylase( Py04_0872) from Pyrococcus sp. ST04
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4cmr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus sp. ST04]]
[[Category: Jung J-H]]
[[Category: Park C-S]]
[[Category: Park K-H]]
[[Category: Woo E-J]]

Latest revision as of 09:25, 17 October 2024

The crystal structure of novel exo-type maltose-forming amylase(Py04_0872) from Pyrococcus sp. ST04The crystal structure of novel exo-type maltose-forming amylase(Py04_0872) from Pyrococcus sp. ST04

Structural highlights

4cmr is a 2 chain structure with sequence from Pyrococcus sp. ST04. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

I3RE04_9EURY

Publication Abstract from PubMed

A novel maltose-forming alpha-amylase (PSMA) was recently found in the hyperthermophilic archaeon Pyrococcus sp. ST04. This enzyme shows <13% amino-acid sequence identity to other known alpha-amylases and displays a unique enzymatic property in that it hydrolyzes both alpha-1,4-glucosidic and alpha-1,6-glucosidic linkages of substrates, recognizing only maltose units, in an exo-type manner. Here, the crystal structure of PSMA at a resolution of 1.8 A is reported, showing a tight ring-shaped tetramer with monomers composed of two domains: an N-domain (amino acids 1-341) with a typical GH57 family (beta/alpha)7-barrel fold and a C-domain (amino acids 342-597) composed of alpha-helical bundles. A small closed cavity observed in proximity to the catalytic residues Glu153 and Asp253 at the domain interface has the appropriate volume and geometry to bind a maltose unit, accounting for the selective exo-type maltose hydrolysis of the enzyme. A narrow gate at the putative subsite +1 formed by residue Phe218 and Phe452 is essential for specific cleavage of glucosidic bonds. The closed cavity at the active site is connected to a short substrate-binding channel that extends to the central hole of the tetramer, exhibiting a geometry that is significantly different from classical maltogenic amylases or beta-amylases. The structural features of this novel exo-type maltose-forming alpha-amylase provide a molecular basis for its unique enzymatic characteristics and for its potential use in industrial applications and protein engineering.

Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04.,Park KH, Jung JH, Park SG, Lee ME, Holden JF, Park CS, Woo EJ Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1659-68. doi:, 10.1107/S1399004714006567. Epub 2014 May 30. PMID:24914977[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Park KH, Jung JH, Park SG, Lee ME, Holden JF, Park CS, Woo EJ. Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04. Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1659-68. doi:, 10.1107/S1399004714006567. Epub 2014 May 30. PMID:24914977 doi:http://dx.doi.org/10.1107/S1399004714006567

4cmr, resolution 1.80Å

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