5TKF

Neurospora crassa polysaccharide monooxygenase 2 high mannosylation

Summary for 5TKF

• Entry DOI: 10.2210/pdb5tkf/pdb
• Related: 5TKg 5TKh 5TKI
• Descriptor: Lytic polysaccharide monooxygenase, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: oxidoreductase, polysaccharide monooxygenase
• Biological source: Neurospora crassa
• Total number of polymer chains: 4
• Total formula weight: 96143.99

Authors

O'Dell, W.B.,Meilleur, F. (deposition date: 2016-10-06, release date: 2017-05-17, Last modification date: 2024-11-20)

Primary citation

O'Dell, W.B.,Swartz, P.D.,Weiss, K.L.,Meilleur, F.
Crystallization of a fungal lytic polysaccharide monooxygenase expressed from glycoengineered Pichia pastoris for X-ray and neutron diffraction.
Acta Crystallogr F Struct Biol Commun, 73:70-78, 2017

PubMed Abstract: Lytic polysaccharide monooxygenases (LPMOs) are carbohydrate-disrupting enzymes secreted by bacteria and fungi that break glycosidic bonds via an oxidative mechanism. Fungal LPMOs typically act on cellulose and can enhance the efficiency of cellulose-hydrolyzing enzymes that release soluble sugars for bioethanol production or other industrial uses. The enzyme PMO-2 from Neurospora crassa (NcPMO-2) was heterologously expressed in Pichia pastoris to facilitate crystallographic studies of the fungal LPMO mechanism. Diffraction resolution and crystal morphology were improved by expressing NcPMO-2 from a glycoengineered strain of P. pastoris and by the use of crystal seeding methods, respectively. These improvements resulted in high-resolution (1.20 Å) X-ray diffraction data collection at 100 K and the production of a large NcPMO-2 crystal suitable for room-temperature neutron diffraction data collection to 2.12 Å resolution.

PubMed: 28177316
DOI: 10.1107/S2053230X16020318

Experimental method

X-RAY DIFFRACTION (2.1 Å)