Triose Phosphate Isomerase

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This page, as it appeared on June 30, 2011, was featured in this article in the journal Biochemistry and Molecular Biology Education.

TPI (yeast) at 2.5 Å resolution (2ypi) dimer. The two identical chains are in grey and green. Ligand is the inhibitor 2-phosphoglycolic acid (PGA).

Drag the structure with the mouse to rotate

Additional Resources

Acknowledgements

The authors of this proteopedia page would like to acknowledge and thank the authors of Triosephosphate Isomerase: Paula Grabowski, Jacqueline Townsend, Kara Pryke, and Regina D. Kettering. Some content from that article was incorporated into the present article.

References

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  2. Harris TK, Abeygunawardana C, Mildvan AS. NMR studies of the role of hydrogen bonding in the mechanism of triosephosphate isomerase. Biochemistry. 1997 Dec 2;36(48):14661-75. PMID:9398185 doi:10.1021/bi972039v
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  17. http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv
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  26. The conservation pattern shown was calculated by ConSurfDB and might obscure some conservation due to inclusion of proteins of different functions. However in the case of 2ypi, all sequences used in the multiple sequence alignment were TPI sequences. A manual run at the ConSurf Server, using 500 TPI sequences, gave a nearly identical result. Both runs gave an average pairwise distance close to 1.0. Hence, the conservation pattern shown is correct for TPI.
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