4lhb
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
{{STRUCTURE_4lhb| PDB=4lhb | SCENE= }} | {{STRUCTURE_4lhb| PDB=4lhb | SCENE= }} | ||
===Crystal structure of tungsten cofactor synthesizing protein MoaB from Pyrococcus furiosus=== | ===Crystal structure of tungsten cofactor synthesizing protein MoaB from Pyrococcus furiosus=== | ||
+ | {{ABSTRACT_PUBMED_24465852}} | ||
==Function== | ==Function== | ||
Line 6: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
- | [[4lhb]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[4lhb]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrfu Pyrfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LHB OCA]. |
+ | |||
+ | ==Reference== | ||
+ | <ref group="xtra">PMID:024465852</ref><references group="xtra"/><references/> | ||
[[Category: Molybdopterin adenylyltransferase]] | [[Category: Molybdopterin adenylyltransferase]] | ||
- | [[Category: | + | [[Category: Pyrfu]] |
[[Category: Havarushka, N.]] | [[Category: Havarushka, N.]] | ||
[[Category: Schwarz, G.]] | [[Category: Schwarz, G.]] | ||
[[Category: Adenylylation of molybdopterin]] | [[Category: Adenylylation of molybdopterin]] | ||
[[Category: Transferase]] | [[Category: Transferase]] |
Revision as of 14:36, 3 March 2014
Contents |
Crystal structure of tungsten cofactor synthesizing protein MoaB from Pyrococcus furiosus
Template:ABSTRACT PUBMED 24465852
Function
[MOAB_PYRFU] Catalyzes the adenylation of molybdopterin as part of the biosynthesis of the molybdenum-cofactor.
About this Structure
4lhb is a 3 chain structure with sequence from Pyrfu. Full crystallographic information is available from OCA.
Reference
- Havarushka N, Fischer-Schrader K, Lamkemeyer T, Schwarz G. Structural Basis of Thermal Stability of the Tungsten Cofactor Synthesis Protein MoaB from Pyrococcus furiosus. PLoS One. 2014 Jan 20;9(1):e86030. doi: 10.1371/journal.pone.0086030. eCollection, 2014 Jan 20. PMID:24465852 doi:http://dx.doi.org/10.1371/journal.pone.0086030