Structural Insights into Radical Generation by the Radical SAM Superfamily
Table of Contents Table of Contents 1. Introduction 2. Unresolved Questions in the Radical SAM Enzyme Field 3. Highlighted Radical SAM Enzymes 3.1. Pyruvate Formate-Lyase Activating Enzyme (PFL-AE) 3.2. Oxygen-Independent Coproporphyrinogen III Oxidase (HemN)...
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Language: | en_US |
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American Chemical Society
2012
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Online Access: | http://hdl.handle.net/1721.1/69646 https://orcid.org/0000-0001-5486-2755 |
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author | Vey, Jessica Lynn Drennan, Catherine L |
author2 | Massachusetts Institute of Technology. Department of Biology |
author_facet | Massachusetts Institute of Technology. Department of Biology Vey, Jessica Lynn Drennan, Catherine L |
author_sort | Vey, Jessica Lynn |
collection | MIT |
description | Table of Contents
Table of Contents
1. Introduction
2. Unresolved Questions in the Radical SAM Enzyme Field
3. Highlighted Radical SAM Enzymes
3.1. Pyruvate Formate-Lyase Activating Enzyme (PFL-AE)
3.2. Oxygen-Independent Coproporphyrinogen III Oxidase (HemN)
3.3. Biotin Synthase (BioB)
3.4. Molybdenum Cofactor Biosynthesis Protein MoaA
3.5. Lysine Aminomutase (LAM)
3.6. Wye-Base Biosynthetic Protein TYW1
3.7. [Fe−Fe] Hydrogenase Maturase Protein HydE
4. Overall Fold
4.1. Radical SAM Core
4.2. Protein Elements Outside of the Radical SAM Core
5. FeS cluster
5.1. Location of the 4Fe−4S Cluster Binding Site
5.2. Environment Surrounding the Cluster
5.3. Interactions between the 4Fe−4S Cluster and AdoMet
6. AdoMet Binding
6.1. AdoMet Conformation
6.2. General Properties of the AdoMet Binding Site
6.3. Overall Description of the AdoMet Binding Site
6.3.1. AdoMet Methionyl Moiety
6.3.2. AdoMet Ribose
6.3.3. AdoMet Adenine Moiety
6.4. AdoMet Binding Motifs in the Radical SAM Superfamily
6.5. Deviations and Variations in AdoMet Binding between the Subfamilies
7. Implications of AdoMet Binding Site Architecture on Function and Reactivity
7.1. Tailoring the Reaction to Specific Substrates
7.2. AdoMet Usage as Cofactor or Cosubstrate
7.3. AdoMet Reaction Stoichiometry
7.4. HemN’s Second AdoMet (SAM2)
8. Substrate Binding to Radical SAM Enzymes
8.1. Positioning of the Substrate
8.2. Additional Cofactors in Some Radical SAM Substrate Binding Sites
8.3. Conformational Changes Associated with Substrate Binding in Radical SAM Enzymes
9. Reductant Binding in Radical SAM Enzymes
10. Other Known AdoMet-Binding Protein Folds
11. Conclusions |
first_indexed | 2024-09-23T13:54:48Z |
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spelling | mit-1721.1/696462022-09-28T17:01:48Z Structural Insights into Radical Generation by the Radical SAM Superfamily Vey, Jessica Lynn Drennan, Catherine L Massachusetts Institute of Technology. Department of Biology Massachusetts Institute of Technology. Department of Chemistry Drennan, Catherine L. Drennan, Catherine L. Vey, Jessica L. Table of Contents Table of Contents 1. Introduction 2. Unresolved Questions in the Radical SAM Enzyme Field 3. Highlighted Radical SAM Enzymes 3.1. Pyruvate Formate-Lyase Activating Enzyme (PFL-AE) 3.2. Oxygen-Independent Coproporphyrinogen III Oxidase (HemN) 3.3. Biotin Synthase (BioB) 3.4. Molybdenum Cofactor Biosynthesis Protein MoaA 3.5. Lysine Aminomutase (LAM) 3.6. Wye-Base Biosynthetic Protein TYW1 3.7. [Fe−Fe] Hydrogenase Maturase Protein HydE 4. Overall Fold 4.1. Radical SAM Core 4.2. Protein Elements Outside of the Radical SAM Core 5. FeS cluster 5.1. Location of the 4Fe−4S Cluster Binding Site 5.2. Environment Surrounding the Cluster 5.3. Interactions between the 4Fe−4S Cluster and AdoMet 6. AdoMet Binding 6.1. AdoMet Conformation 6.2. General Properties of the AdoMet Binding Site 6.3. Overall Description of the AdoMet Binding Site 6.3.1. AdoMet Methionyl Moiety 6.3.2. AdoMet Ribose 6.3.3. AdoMet Adenine Moiety 6.4. AdoMet Binding Motifs in the Radical SAM Superfamily 6.5. Deviations and Variations in AdoMet Binding between the Subfamilies 7. Implications of AdoMet Binding Site Architecture on Function and Reactivity 7.1. Tailoring the Reaction to Specific Substrates 7.2. AdoMet Usage as Cofactor or Cosubstrate 7.3. AdoMet Reaction Stoichiometry 7.4. HemN’s Second AdoMet (SAM2) 8. Substrate Binding to Radical SAM Enzymes 8.1. Positioning of the Substrate 8.2. Additional Cofactors in Some Radical SAM Substrate Binding Sites 8.3. Conformational Changes Associated with Substrate Binding in Radical SAM Enzymes 9. Reductant Binding in Radical SAM Enzymes 10. Other Known AdoMet-Binding Protein Folds 11. Conclusions Massachusetts Institute of Technology (William Asbjornsen Albert Memorial Fellowship) Howard Hughes Medical Institute (Investigator) 2012-03-14T14:06:29Z 2012-03-14T14:06:29Z 2011-03 2009-07 Article http://purl.org/eprint/type/JournalArticle 0009-2665 1520-6890 http://hdl.handle.net/1721.1/69646 Vey, Jessica L., and Catherine L. Drennan. “Structural Insights into Radical Generation by the Radical SAM Superfamily.” Chemical Reviews 111.4 (2011): 2487–2506. https://orcid.org/0000-0001-5486-2755 en_US http://dx.doi.org/10.1021/cr9002616 Chemical Reviews Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf American Chemical Society Prof. Drennan via Erja Kajosalo |
spellingShingle | Vey, Jessica Lynn Drennan, Catherine L Structural Insights into Radical Generation by the Radical SAM Superfamily |
title | Structural Insights into Radical Generation by the Radical SAM Superfamily |
title_full | Structural Insights into Radical Generation by the Radical SAM Superfamily |
title_fullStr | Structural Insights into Radical Generation by the Radical SAM Superfamily |
title_full_unstemmed | Structural Insights into Radical Generation by the Radical SAM Superfamily |
title_short | Structural Insights into Radical Generation by the Radical SAM Superfamily |
title_sort | structural insights into radical generation by the radical sam superfamily |
url | http://hdl.handle.net/1721.1/69646 https://orcid.org/0000-0001-5486-2755 |
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