Structural Characterization of the Active Site of the PduO-Type ATP:Co(I)rrinoid Adenosyltransferase from Lactobacillus reuteri

Maurice, Martin St.; Mera, Paola E.; Taranto, María Pía; Sesma, Fernando; Escalante‐Semerena, Jorge C.; Rayment, Ivan

doi:10.1074/jbc.m609557200

Cited by 65 publications

(144 citation statements)

References 48 publications

(36 reference statements)

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“…2). Another example of functional evidence can be found in the recent report of the crystal structure of the PduO-type ATP : Co(I)rrinoid adenosyltransferase (St Maurice et al, 2007) also sequenced within the course of this study.…”

Section: F Santos and Others 90mentioning

confidence: 60%

The complete coenzyme B12 biosynthesis gene cluster of Lactobacillus reuteri CRL1098

et al. 2008

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Section: F Santos and Others 90mentioning

confidence: 60%

The complete coenzyme B12 biosynthesis gene cluster of Lactobacillus reuteri CRL1098

et al. 2008

Self Cite

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“…In vitro studies indicate that the substrate of PduS is cob(II)alamin bound to an ATR. When cob(II)alamin binds ATR, it undergoes a transition to the 4-coordinate base-off conformer (132)(133)(134)(135). Transition to this state raises the midpoint potential of the cob(II)alamin/cob(I)alamin couple by about 250 mV, facilitating reduction.…”

Section: Enzymes For Reactivation Of Diol Dehydratase and B 12 Recyclingmentioning

confidence: 99%

“…The C-terminal domain (about 150 amino acids in length) is a widely conserved domain of unknown function (DUF336). Although the three-dimensional structure of PduO of Salmonella has not been characterized, crystal structures for the PduO N-terminal ATR domains from Lactobacillus reuteri and several other organism have been reported (133,139,140). For Lactobacillus, cocrystallization of the PduO protein with ATP and cob(II)alamin reveals the molecular features of four-coordinate cob(II)alamin stabilization at its active site, where the corrin ring is found in a hydrophobic environment (133,139) (Fig.…”

Section: Enzymes For Reactivation Of Diol Dehydratase and B 12 Recyclingmentioning

confidence: 99%

Diverse Bacterial Microcompartment Organelles

Chowdhury

Sinha

Chun

et al. 2014

Microbiol Mol Biol Rev

207

278

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SUMMARY Bacterial microcompartments (MCPs) are sophisticated protein-based organelles used to optimize metabolic pathways. They consist of metabolic enzymes encapsulated within a protein shell, which creates an ideal environment for catalysis and facilitates the channeling of toxic/volatile intermediates to downstream enzymes. The metabolic processes that require MCPs are diverse and widely distributed and play important roles in global carbon fixation and bacterial pathogenesis. The protein shells of MCPs are thought to selectively control the movement of enzyme cofactors, substrates, and products (including toxic or volatile intermediates) between the MCP interior and the cytoplasm of the cell using both passive electrostatic/steric and dynamic gated mechanisms. Evidence suggests that specialized shell proteins conduct electrons between the cytoplasm and the lumen of the MCP and/or help rebuild damaged iron-sulfur centers in the encapsulated enzymes. The MCP shell is elaborated through a family of small proteins whose structural core is known as a bacterial microcompartment (BMC) domain. BMC domain proteins oligomerize into flat, hexagonally shaped tiles, which assemble into extended protein sheets that form the facets of the shell. Shape complementarity along the edges allows different types of BMC domain proteins to form mixed sheets, while sequence variation provides functional diversification. Recent studies have also revealed targeting sequences that mediate protein encapsulation within MCPs, scaffolding proteins that organize lumen enzymes and the use of private cofactor pools (NAD/H and coenzyme A [HS-CoA]) to facilitate cofactor homeostasis. Although much remains to be learned, our growing understanding of MCPs is providing a basis for bioengineering of protein-based containers for the production of chemicals/pharmaceuticals and for use as molecular delivery vehicles.

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“…CN-Cbl is first reductively decyanated to cob(II)alamin (22,30,68). Next, cob(II)alamin is reduced to cob(I)alamin, and ATP:cob(I)alamin adenosyltransferase (ATR) transfers a 5Ј deoxyadenosyl group from ATP to cob(I)alamin to form AdoCbl (10,11,28,29,35,63,64,72). Studies indicate that prior to reduction cob(II)alamin binds the ATR and undergoes a transition to the 4-coordinate base-off conformer (41,48,59,61,62).…”

mentioning

confidence: 99%

Characterization of the PduS Cobalamin Reductase of Salmonella enterica and Its Role in the Pdu Microcompartment

Cheng

Bobik

2010

J Bacteriol

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Structural Characterization of the Active Site of the PduO-Type ATP:Co(I)rrinoid Adenosyltransferase from Lactobacillus reuteri

Abstract: The three-dimensional crystal structure of the PduO-type corrinoid adenosyltransferase from Lactobacillus reuteri

Cited by 65 publications

References 48 publications

The complete coenzyme B12 biosynthesis gene cluster of Lactobacillus reuteri CRL1098

The complete coenzyme B12 biosynthesis gene cluster of Lactobacillus reuteri CRL1098

Diverse Bacterial Microcompartment Organelles

Characterization of the PduS Cobalamin Reductase of Salmonella enterica and Its Role in the Pdu Microcompartment

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