2bm3: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 5: | Line 5: | ||
==Overview== | ==Overview== | ||
The plant cell wall degrading enzymes expressed by anaerobic, microorganisms form large multienzyme complexes (cellulosomes)., Cellulosomes assemble by the Type I dockerins on the catalytic subunits, binding to the reiterated Type I cohesins in the molecular scaffold, while, Type II dockerin-cohesin interactions anchor the complex onto the, bacterial cell surface. Type I and Type II cohesin, dockerin pairs show no, cross-specificity. Here we report the crystal structure of the Type II, cohesin (CohII) from the Clostridium thermocellum cell surface anchoring, protein SdbA. The protein domain contains nine beta-strands and a small, alpha-helix. The beta-strands assemble into two elongated beta-sheets that, display a typical jelly roll fold. The structure of CohII is very similar, to Type I .. | The plant cell wall degrading enzymes expressed by anaerobic, microorganisms form large multienzyme complexes (cellulosomes)., Cellulosomes assemble by the Type I dockerins on the catalytic subunits, binding to the reiterated Type I cohesins in the molecular scaffold, while, Type II dockerin-cohesin interactions anchor the complex onto the, bacterial cell surface. Type I and Type II cohesin, dockerin pairs show no, cross-specificity. Here we report the crystal structure of the Type II, cohesin (CohII) from the Clostridium thermocellum cell surface anchoring, protein SdbA. The protein domain contains nine beta-strands and a small, alpha-helix. The beta-strands assemble into two elongated beta-sheets that, display a typical jelly roll fold. The structure of CohII is very similar, to Type I cohesins, and the dockerin binding site, which is centred at, beta-strands 3, 5 and 6, is likely to be conserved in the two proteins., Subtle differences in the topology of the binding sites and a lack of, sequence identity in the beta-strands that comprise the core of the, dockerin binding site explain why Type I and Type II cohesins display such, distinct specificities for their target dockerins. | ||
==About this Structure== | ==About this Structure== | ||
2BM3 is a | 2BM3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum] with IPA as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BM3 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 32: | Line 32: | ||
[[Category: type 2]] | [[Category: type 2]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:44:11 2007'' | ||
