Domain alternation switches B12-dependent methionine synthase to the activation conformation
B 12 -dependent methionine synthase (MetH) from Escherichia coli is a large modular protein that uses bound cobalamin as an intermediate methyl carrier. Major domain rearrangements have been postulated to explain how cobalamin reacts with three different substrates: homocysteine, methyltetrahydrofol...
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| Veröffentlicht in: | Nature Structural Biology 2002-01, Vol.9 (1), p.53-56 |
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| creator | Bandarian, Vahe Pattridge, Katherine A. Lennon, Brett W. Huddler, Donald P. Matthews, Rowena G. Ludwig, Martha L. |
| description | B
12
-dependent methionine synthase (MetH) from
Escherichia coli
is a large modular protein that uses bound cobalamin as an intermediate methyl carrier. Major domain rearrangements have been postulated to explain how cobalamin reacts with three different substrates: homocysteine, methyltetrahydrofolate and S-adenosylmethionine (AdoMet). Here we describe the 3.0 Å structure of a 65 kDa C-terminal fragment of MetH that spans the cobalamin- and AdoMet-binding domains, arranged in a conformation suitable for the methyl transfer from AdoMet to cobalamin that occurs during activation. In the conversion to the activation conformation, a helical domain that capped the cofactor moves 26 Å and rotates by 63°, allowing formation of a new interface between cobalamin and the AdoMet-binding (activation) domain. Interactions with the MetH activation domain drive the cobalamin away from its binding domain in a way that requires dissociation of the axial cobalt ligand and, thereby, provide a mechanism for control of the distribution of enzyme conformations. |
| doi_str_mv | 10.1038/nsb738 |
| format | Article |
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12
-dependent methionine synthase (MetH) from
Escherichia coli
is a large modular protein that uses bound cobalamin as an intermediate methyl carrier. Major domain rearrangements have been postulated to explain how cobalamin reacts with three different substrates: homocysteine, methyltetrahydrofolate and S-adenosylmethionine (AdoMet). Here we describe the 3.0 Å structure of a 65 kDa C-terminal fragment of MetH that spans the cobalamin- and AdoMet-binding domains, arranged in a conformation suitable for the methyl transfer from AdoMet to cobalamin that occurs during activation. In the conversion to the activation conformation, a helical domain that capped the cofactor moves 26 Å and rotates by 63°, allowing formation of a new interface between cobalamin and the AdoMet-binding (activation) domain. Interactions with the MetH activation domain drive the cobalamin away from its binding domain in a way that requires dissociation of the axial cobalt ligand and, thereby, provide a mechanism for control of the distribution of enzyme conformations.</description><identifier>ISSN: 1072-8368</identifier><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsb738</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Biochemistry ; Biological Microscopy ; Biomedical and Life Sciences ; Cobalt ; E coli ; letter ; Life Sciences ; Membrane Biology ; Protein Structure</subject><ispartof>Nature Structural Biology, 2002-01, Vol.9 (1), p.53-56</ispartof><rights>Springer Nature America, Inc. 2001</rights><rights>Copyright Nature Publishing Group Jan 2002</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2618-1dcaf2461c60333f99477095f314d6397953a840bb7a51be2041783284004853</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Bandarian, Vahe</creatorcontrib><creatorcontrib>Pattridge, Katherine A.</creatorcontrib><creatorcontrib>Lennon, Brett W.</creatorcontrib><creatorcontrib>Huddler, Donald P.</creatorcontrib><creatorcontrib>Matthews, Rowena G.</creatorcontrib><creatorcontrib>Ludwig, Martha L.</creatorcontrib><title>Domain alternation switches B12-dependent methionine synthase to the activation conformation</title><title>Nature Structural Biology</title><addtitle>Nat Struct Mol Biol</addtitle><description>B
12
-dependent methionine synthase (MetH) from
Escherichia coli
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12
-dependent methionine synthase (MetH) from
Escherichia coli
is a large modular protein that uses bound cobalamin as an intermediate methyl carrier. Major domain rearrangements have been postulated to explain how cobalamin reacts with three different substrates: homocysteine, methyltetrahydrofolate and S-adenosylmethionine (AdoMet). Here we describe the 3.0 Å structure of a 65 kDa C-terminal fragment of MetH that spans the cobalamin- and AdoMet-binding domains, arranged in a conformation suitable for the methyl transfer from AdoMet to cobalamin that occurs during activation. In the conversion to the activation conformation, a helical domain that capped the cofactor moves 26 Å and rotates by 63°, allowing formation of a new interface between cobalamin and the AdoMet-binding (activation) domain. Interactions with the MetH activation domain drive the cobalamin away from its binding domain in a way that requires dissociation of the axial cobalt ligand and, thereby, provide a mechanism for control of the distribution of enzyme conformations.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><doi>10.1038/nsb738</doi><tpages>4</tpages></addata></record> |
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| subjects | Biochemistry Biological Microscopy Biomedical and Life Sciences Cobalt E coli letter Life Sciences Membrane Biology Protein Structure |
| title | Domain alternation switches B12-dependent methionine synthase to the activation conformation |
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