3gaj

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(New page: '''Unreleased structure''' The entry 3gaj is ON HOLD Authors: St Maurice, M., Mera, P.E., Escalante-Semerena, J.C., Rayment, I. Description: Structure of a C-terminal deletion variant ...)
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'''Unreleased structure'''
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{{Seed}}
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[[Image:3gaj.jpg|left|200px]]
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The entry 3gaj is ON HOLD
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{{STRUCTURE_3gaj| PDB=3gaj | SCENE= }}
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Authors: St Maurice, M., Mera, P.E., Escalante-Semerena, J.C., Rayment, I.
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===Structure of a C-terminal deletion variant of a PduO-type ATP:corrinoid adenosyltransferase from Lactobacillus reuteri complexed with cobalamin and ATP===
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Description: Structure of a C-terminal deletion variant of a PduO-type ATP:corrinoid adenosyltransferase from Lactobacillus reuteri complexed with cobalamin and ATP
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 4 14:46:00 2009''
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{{ABSTRACT_PUBMED_19236001}}
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==About this Structure==
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3GAJ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_reuteri Lactobacillus reuteri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GAJ OCA].
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==Reference==
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<ref group="xtra">PMID:19236001</ref><references group="xtra"/>
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[[Category: Lactobacillus reuteri]]
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[[Category: Escalante-Semerena, J C.]]
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[[Category: Maurice, M St.]]
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[[Category: Mera, P E.]]
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[[Category: Rayment, I.]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 8 09:28:45 2009''

Revision as of 06:28, 8 July 2009

Template:STRUCTURE 3gaj

Structure of a C-terminal deletion variant of a PduO-type ATP:corrinoid adenosyltransferase from Lactobacillus reuteri complexed with cobalamin and ATP

Template:ABSTRACT PUBMED 19236001

About this Structure

3GAJ is a 1 chain structure of sequence from Lactobacillus reuteri. Full crystallographic information is available from OCA.

Reference

  • Mera PE, St Maurice M, Rayment I, Escalante-Semerena JC. Residue Phe112 of the human-type corrinoid adenosyltransferase (PduO) enzyme of Lactobacillus reuteri is critical to the formation of the four-coordinate Co(II) corrinoid substrate and to the activity of the enzyme. Biochemistry. 2009 Apr 14;48(14):3138-45. PMID:19236001 doi:10.1021/bi9000134

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