2e9b: Difference between revisions

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|PDB= 2e9b |SIZE=350|CAPTION= <scene name='initialview01'>2e9b</scene>, resolution 2.30&Aring;
|PDB= 2e9b |SIZE=350|CAPTION= <scene name='initialview01'>2e9b</scene>, resolution 2.30&Aring;
|SITE= <scene name='pdbsite=AC1:Glc+Binding+Site+For+Residue+A+721'>AC1</scene>, <scene name='pdbsite=AC2:Glc+Binding+Site+For+Residue+A+722'>AC2</scene>, <scene name='pdbsite=AC3:Glc+Binding+Site+For+Residue+A+723'>AC3</scene>, <scene name='pdbsite=AC4:Glc+Binding+Site+For+Residue+B+731'>AC4</scene>, <scene name='pdbsite=AC5:Glc+Binding+Site+For+Residue+B+732'>AC5</scene>, <scene name='pdbsite=AC6:Glc+Binding+Site+For+Residue+B+733'>AC6</scene>, <scene name='pdbsite=AC7:Glc+Binding+Site+For+Residue+A+735'>AC7</scene>, <scene name='pdbsite=AC8:Glc+Binding+Site+For+Residue+A+736'>AC8</scene>, <scene name='pdbsite=AC9:Ca+Binding+Site+For+Residue+A+741'>AC9</scene>, <scene name='pdbsite=BC1:Ca+Binding+Site+For+Residue+B+742'>BC1</scene>, <scene name='pdbsite=BC2:Act+Binding+Site+For+Residue+A+751'>BC2</scene>, <scene name='pdbsite=BC3:Act+Binding+Site+For+Residue+B+752'>BC3</scene>, <scene name='pdbsite=BC4:Gol+Binding+Site+For+Residue+A+761'>BC4</scene> and <scene name='pdbsite=BC5:Gol+Binding+Site+For+Residue+B+762'>BC5</scene>
|SITE= <scene name='pdbsite=AC1:Glc+Binding+Site+For+Residue+A+721'>AC1</scene>, <scene name='pdbsite=AC2:Glc+Binding+Site+For+Residue+A+722'>AC2</scene>, <scene name='pdbsite=AC3:Glc+Binding+Site+For+Residue+A+723'>AC3</scene>, <scene name='pdbsite=AC4:Glc+Binding+Site+For+Residue+B+731'>AC4</scene>, <scene name='pdbsite=AC5:Glc+Binding+Site+For+Residue+B+732'>AC5</scene>, <scene name='pdbsite=AC6:Glc+Binding+Site+For+Residue+B+733'>AC6</scene>, <scene name='pdbsite=AC7:Glc+Binding+Site+For+Residue+A+735'>AC7</scene>, <scene name='pdbsite=AC8:Glc+Binding+Site+For+Residue+A+736'>AC8</scene>, <scene name='pdbsite=AC9:Ca+Binding+Site+For+Residue+A+741'>AC9</scene>, <scene name='pdbsite=BC1:Ca+Binding+Site+For+Residue+B+742'>BC1</scene>, <scene name='pdbsite=BC2:Act+Binding+Site+For+Residue+A+751'>BC2</scene>, <scene name='pdbsite=BC3:Act+Binding+Site+For+Residue+B+752'>BC3</scene>, <scene name='pdbsite=BC4:Gol+Binding+Site+For+Residue+A+761'>BC4</scene> and <scene name='pdbsite=BC5:Gol+Binding+Site+For+Residue+B+762'>BC5</scene>
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Pullulanase Pullulanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.41 3.2.1.41]  
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pullulanase Pullulanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.41 3.2.1.41] </span>
|GENE= amyX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
|GENE= amyX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
|DOMAIN=
|RELATEDENTRY=[[2e8y|2E8Y]], [[2e8z|2E8Z]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e9b OCA], [http://www.ebi.ac.uk/pdbsum/2e9b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2e9b RCSB]</span>
}}
}}


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[[Category: Mikami, B.]]
[[Category: Mikami, B.]]
[[Category: Utsumi, S.]]
[[Category: Utsumi, S.]]
[[Category: ACT]]
[[Category: CA]]
[[Category: GOL]]
[[Category: alpha-amylase-family maltose]]
[[Category: alpha-amylase-family maltose]]
[[Category: beta-alpha-barrel]]
[[Category: beta-alpha-barrel]]
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[[Category: smultiple domain]]
[[Category: smultiple domain]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:37:04 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:45:42 2008''

Revision as of 02:45, 31 March 2008

File:2e9b.jpg


PDB ID 2e9b

Drag the structure with the mouse to rotate
, resolution 2.30Å
Sites: , , , , , , , , , , , , and
Ligands: , , , ,
Gene: amyX (Bacillus subtilis)
Activity: Pullulanase, with EC number 3.2.1.41
Related: 2E8Y, 2E8Z


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with maltose


OverviewOverview

The AmyX gene encoding pullulanase from the common spore-forming bacterium Bacillus subtilis strain 168 was cloned, overexpressed in Escherichia coli, purified and crystallized. The recombinant pullulanase was purified to homogeneity using ammonium sulfate precipitation, hydrophobic chromatography and anion-exchange chromatography, resulting in a specific activity of 24.10 U per milligram of protein. SDS-PAGE analysis showed that the molecular weight of the protein is approximately 81.0 kDa, which is similar to the calculated molecular weight, 81.1 kDa, from its translated cDNA sequence. The k(cat) and K(m) of the purified enzyme with pullulan as substrate were approximately 79 s(-1) and 1.284 mg ml(-1), respectively. X-ray crystallographic analysis of the pullulanase crystal showed that the crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 70.568, b = 127.68, c = 189.25 angstroms. The crystal contains two molecules of pullulanase in the asymmetric unit, with a solvent content of 53.15%. The crystal diffracted to 2.1 angstroms resolution at a synchrotron and is suitable for structure determination.

About this StructureAbout this Structure

2E9B is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

ReferenceReference

Overexpression, purification and preliminary X-ray analysis of pullulanase from Bacillus subtilis strain 168., Malle D, Itoh T, Hashimoto W, Murata K, Utsumi S, Mikami B, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt, 4):381-4. Epub 2006 Mar 25. PMID:16582490

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