4iz6

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'''Unreleased structure'''
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{{STRUCTURE_4iz6| PDB=4iz6 | SCENE= }}
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===Structure of EntE and EntB, an NRPS adenylation-PCP fusion protein with pseudo translational symmetry===
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The entry 4iz6 is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/ENTE_ECOLI ENTE_ECOLI]] Activates the carboxylate group of 2,3-dihydroxy-benzoate (2,3-DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate. Then, catalyzes the acylation of holo-EntB with 2,3-DHB adenylate, preparing that molecule for amide bond formation with L-serine.
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Authors: Gulick, A.M., Sundlov, J.A.
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==About this Structure==
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[[4iz6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IZ6 OCA].
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Description: Structure of EntE and EntB, an NRPS adenylation-PCP fusion protein with pseudo translational symmetry
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[[Category: Escherichia coli]]
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[[Category: Gulick, A M.]]
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[[Category: Sundlov, J A.]]
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[[Category: 4'phosphopantetheinylation cofactor 4'pp]]
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[[Category: Acyl carrier protein]]
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[[Category: Adenylate-forming enzyme]]
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[[Category: Anl superfamily]]
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[[Category: Chimera protein]]
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[[Category: Fusion protein]]
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[[Category: Ligase]]
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[[Category: Non-ribosomal peptide synthetase]]
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[[Category: Nrps adenylation domains and acyl carrier protein domain]]
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[[Category: Pseudo-translational symmetry]]

Revision as of 05:19, 1 August 2013

Template:STRUCTURE 4iz6

Structure of EntE and EntB, an NRPS adenylation-PCP fusion protein with pseudo translational symmetry

Function

[ENTE_ECOLI] Activates the carboxylate group of 2,3-dihydroxy-benzoate (2,3-DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate. Then, catalyzes the acylation of holo-EntB with 2,3-DHB adenylate, preparing that molecule for amide bond formation with L-serine.

About this Structure

4iz6 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

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