6N99

Xylose isomerase 2F1 variant from Streptomyces sp. F-1

Summary for 6N99

• Entry DOI: 10.2210/pdb6n99/pdb
• Descriptor: Xylose isomerase, MAGNESIUM ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: wild type, isomerase
• Biological source: Streptomyces sp. F-1
• Total number of polymer chains: 4
• Total formula weight: 172308.32

Authors

Miyamoto, R.Y.,Vieira, P.S.,Murakami, M.T.,Zanphorlin, L.M. (deposition date: 2018-12-01, release date: 2019-12-04, Last modification date: 2023-10-11)

Primary citation

Miyamoto, R.Y.,de Sousa, A.S.,Vieira, P.S.,de Melo, R.R.,Scarpassa, J.A.,Ramos, C.H.I.,Murakami, M.T.,Ruller, R.,Zanphorlin, L.M.
Crystal structure of a novel xylose isomerase from Streptomyces sp. F-1 revealed the presence of unique features that differ from conventional classes.
Biochim Biophys Acta Gen Subj, 1864:129549-129549, 2020

PubMed Abstract: Enzymatic isomerization is a promising strategy to solve the problem of xylose fermentation and, consequently, to leverage the production of advanced biofuels and biochemicals. In a previous work, our research group discovered a new strain of Streptomyces with great biotechnological potential due to its ability to produce a broad arsenal of enzymes related to lignocellulose degradation.

PubMed: 32035160
DOI: 10.1016/j.bbagen.2020.129549

Experimental method

X-RAY DIFFRACTION (2.8 Å)