View source for 3vm7


==Structure of an Alpha-Amylase from Malbranchea cinnamomea==
<StructureSection load='3vm7' size='340' side='right'caption='[[3vm7]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3vm7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Malbranchea_cinnamomea Malbranchea cinnamomea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VM7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VM7 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]] 2.25&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=3vm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vm7 OCA], [https://pdbe.org/3vm7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vm7 RCSB], [https://www.ebi.ac.uk/pdbsum/3vm7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vm7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/K9L8F3_MALCI K9L8F3_MALCI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A novel alpha-amylase (McAmyA) from the thermophilic fungus, Malbranchea cinnamomea was purified, characterized and crystallized in the present study. McAmyA was purified to apparent homogeneity with a molecular mass of 60.3 kDa on SDS-PAGE. The enzyme exhibited maximal activity at pH 6.5 and was stable within pH 5.0-10.0. It was most active at 65 degrees C and was stable up to 50 degrees C. McAmyA was capable of hydrolyzing amylose, starch, amylopectin, pullulan, cyclodextrins and maltooligosaccharides. The full-length cDNA of an alpha-amylase gene (McAmyA) from the strain was cloned. McAmyA consisted of a 1,476-bp open reading frame encoding 492 amino acids. It displayed the highest amino acid sequence homology (less than 60 %) with the reported alpha-amylases. The crystal structure of McAmyA was solved at a resolution of 2.25 A (PDB code 3VM7). The overall structure of McAmyA reveals three domains with ten alpha helices and 14 beta strands, and the putative catalytic residues are positioned at domain A with somewhat different secondary structural circumstances compared with typical alpha-amylases.

A novel multifunctional alpha-amylase from the thermophilic fungus Malbranchea cinnamomea: biochemical characterization and three-dimensional structure.,Han P, Zhou P, Hu S, Yang S, Yan Q, Jiang Z Appl Biochem Biotechnol. 2013 May;170(2):420-35. doi: 10.1007/s12010-013-0198-y. , Epub 2013 Mar 29. PMID:23536251<ref>PMID:23536251</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3vm7" style="background-color:#fffaf0;"></div>

==See Also==
*[[Amylase 3D structures|Amylase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Malbranchea cinnamomea]]
[[Category: Han P]]
[[Category: Hu SQ]]
[[Category: Jiang ZQ]]
[[Category: Yang SQ]]
[[Category: Zhou P]]
[[Category: Zhou Y]]