2jie: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:2jie.jpg|left|200px]]<br /><applet load="2jie" size=" | [[Image:2jie.jpg|left|200px]]<br /><applet load="2jie" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2jie, resolution 2.3Å" /> | caption="2jie, resolution 2.3Å" /> | ||
'''BETA-GLUCOSIDASE B FROM BACILLUS POLYMYXA COMPLEXED WITH 2-F-GLUCOSE'''<br /> | '''BETA-GLUCOSIDASE B FROM BACILLUS POLYMYXA COMPLEXED WITH 2-F-GLUCOSE'''<br /> | ||
Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
2JIE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paenibacillus_polymyxa Paenibacillus polymyxa] with G2F as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] Known structural/functional Site: <scene name='pdbsite=AC1:G2f Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | 2JIE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paenibacillus_polymyxa Paenibacillus polymyxa] with <scene name='pdbligand=G2F:'>G2F</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] Known structural/functional Site: <scene name='pdbsite=AC1:G2f Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JIE OCA]. | ||
==Reference== | ==Reference== | ||
Line 27: | Line 27: | ||
[[Category: polysaccharide degradation]] | [[Category: polysaccharide degradation]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:56:16 2008'' |
Revision as of 14:56, 23 January 2008
|
BETA-GLUCOSIDASE B FROM BACILLUS POLYMYXA COMPLEXED WITH 2-F-GLUCOSE
OverviewOverview
Bacteria species involved in degradation of cellulosic substrates produce, a variety of enzymes for processing related compounds along the hydrolytic, pathway. Paenibacillus polymyxa encodes two homologous beta-glucosidases, BglA and BglB, presenting different quaternary structures and substrate, specificities. We previously reported the 3D-structure of BglA, which is, highly specific against cellobiose. Here, we present structural analysis, of BglB, a monomeric enzyme that acts as an exo-beta-glucosidase, hydrolyzing cellobiose and cellodextrins of higher degree of, polymerization. The crystal structure of BglB shows that several polar, residues narrow the active site pocket and contour additional subsites., The structure of the BglB-cellotetraose complex confirms these subsites, revealing the substrate-binding mode, and shows the oligosaccharide-enzyme, recognition pattern in detail. Comparison between BglA and BglB crystal, structures suggests that oligomerization in BglA can assist in fine-tuning, the specificity of the active centre by modulating the loops surrounding, the cavity. We have solved the crystal structure of BglB with bound, thiocellobiose, a competitive inhibitor, which together with the, BglB-cellotetraose complex delineate the general features of the aglycon, site. The detailed characterization of the atomic interactions at the, aglycon site show a recognition pattern common to all bacterial, beta-glucosidases, and presents some differences with the aglycon site in, plant beta-glycosidases essentially by means of a different orientation of, the basal Trp. The crystal structures of of BglB with a covalently bound, inhibitor (derived from 2-fluoroglucoside) and glucose (produced by, hydrolysis of the substrate in the crystal), provide additional pictures, of the binding events and the intermediates formed during the reaction., Altogether, this information can assist in the understanding of subtle, differences of the enzyme mechanism and substrate recognition within this, family of enzymes, and consequently it can help in the development of new, enzymes with improved activity or specificity.
About this StructureAbout this Structure
2JIE is a Single protein structure of sequence from Paenibacillus polymyxa with as ligand. Active as Beta-glucosidase, with EC number 3.2.1.21 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Crystal Structures of Paenibacillus polymyxa beta-Glucosidase B Complexes Reveal the Molecular Basis of Substrate Specificity and Give New Insights into the Catalytic Machinery of Family I Glycosidases., Isorna P, Polaina J, Latorre-Garcia L, Canada FJ, Gonzalez B, Sanz-Aparicio J, J Mol Biol. 2007 Aug 31;371(5):1204-18. Epub 2007 Jun 2. PMID:17585934
Page seeded by OCA on Wed Jan 23 13:56:16 2008