Crystal structure of auxin-binding protein 1 in complex with auxin

Woo, Eui-Jeon; Marshall, J.; Bauly, James; Chen, Jay; Venis, Michael A.; Napier, Richard; Pickersgill, Richard W.

doi:10.1093/emboj/cdf291

Cited by 147 publications

(174 citation statements)

References 45 publications

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“…The biochemical properties of this binding activity were characterized Ray, 1977;Venis, 1977), but it was not until 1985 that Zm-ABP1 protein was purified (Lö bler and Klä mbt, 1985) and subsequently molecularly cloned Inohara et al, 1989;Tillmann et al, 1989). In the same year, it was also proven that ABP1 indeed binds auxin (Jones and Venis, 1989), a result that was later corroborated by the crystal structure determination of ABP1 cocrystallized with auxin (Woo et al 2002). ABP1 antibodies and peptides generated in these biochemical studies were increasingly used for physiological studies in heterologous systems, showing auxin induction of cellular processes such as membrane hyperpolarization (Barbier-Brygoo et al, 1991;Venis et al, 1992), K + fluxes (Thiel et al, 1993), or cell expansion, as evidenced by protoplast swelling assays (Steffens et al, 2001).…”

Section: Timeline Of Abp1 Researchmentioning

confidence: 99%

AUXIN BINDING PROTEIN1: The Outsider

2011

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AUXIN BINDING PROTEIN1 (ABP1) is one of the first characterized proteins that bind auxin and has been implied as a receptor for a number of auxin responses. Early studies characterized its auxin binding properties and focused on rapid electrophysiological and cell expansion responses, while subsequent work indicated a role in cell cycle and cell division control. Very recently, ABP1 has been ascribed a role in modulating endocytic events at the plasma membrane and RHO OF PLANTS-mediated cytoskeletal rearrangements during asymmetric cell expansion. The exact molecular function of ABP1 is still unresolved, but its main activity apparently lies in influencing events at the plasma membrane. This review aims to connect the novel findings with the more classical literature on ABP1 and to point out the many open questions that still separate us from a comprehensive model of ABP1 action, almost 40 years after the first reports of its existence.

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Section: Timeline Of Abp1 Researchmentioning

confidence: 99%

AUXIN BINDING PROTEIN1: The Outsider

2011

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“…The average metal-nitrogen distance is 2.08 Å, and the metal-water distance is 2.13 Å. The Zn 2+ ligands are part of the conserved metal binding motifs GX 5 HXH(X) 3,4 EX 6 G and GX 5 PXGX 2 HX 3 N characteristic for the cupin fold [28]. In RemF they are modified to GX 5 HXHX 3 HX 6 G and GX 5 PXGX 2 HX 3 T (deviations from the canonical cupin fingerprints indicated in bold).…”

Section: The Metal Binding Site In Remfmentioning

confidence: 99%

The polyketide cyclase RemF from Streptomyces resistomycificus contains an unusual octahedral zinc binding site

2009

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a b s t r a c tRemF is a polyketide cyclase involved in the biosynthesis of the aromatic pentacyclic metabolite resistomycin in Streptomyces resistomycificus. The enzyme is a member of a structurally hitherto uncharacterized class of polyketide cyclases. The crystal structure of RemF was determined by SAD and refined to 1.2 Å resolution. The enzyme subunit shows a b-sandwich structure with a topology characteristic for the cupin fold. RemF contains a metal binding site located at the bottom of the predominantly hydrophobic active site cavity. A zinc ion is coordinated to four histidine side chains, and two water molecules in octahedral ligand sphere geometry, highly unusual for zinc binding sites in proteins.

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“…These studies can suggest a pharmacophoric model to develop new active compounds more selective and effective against witches' broom. The release of MP-CPY51, which has 555 amino acids, motivates us to build a model (WOO et al, 2002). Next, BLASTp (ALTSCHUL et al, 1990) server was used to identify sequences homologous to MP-CYP51.…”

Section: Introductionmentioning

confidence: 99%

Estudos de Modelagem Comparativa da lanosterol 14-alfa demetilase de Moniliophthora perniciosa

Pacheco¹,

Castilho²,

Lucchese³

et al. 2013

BBR - Biochem. Biotechnol.

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Moniliophthora perniciosa is the causative agent of witches' broom, which affects the Theobroma cacao, causing great losses in cocoa production. The integrated management techniques available allow controlling the pest only partially. An important strategy to contain the witches' broom is to study the interactions of the enzyme lanosterol 14α-demethylase (CYP51) of Moniliophthora with azole compounds. These compounds block the synthesis of ergosterol and consequently the fungal growth by the connection between the iron atom in the cofactor of this enzyme and the nitrogen atom of the azole. However, there is no study on the interaction of these compounds with the enzyme lanosterol 14α-demethylase of this pathogen. In this work, a model of the enzyme lanosterol 14α-demethylase of M. perniciosa was created by comparative modeling techniques. Then, the spatial arrangement of residues that comprise the catalytic site of the enzyme was identified. The results obtained are in agreement with the RESUMOMoniliophthora perniciosa é o agente causador da vassoura de bruxa, que afeta o Theobroma cacao, causando grandes perdas na produção de cacau. As técnicas de gestão integrada desenvolvidas permitem controlar a praga apenas parcialmente. Uma estratégia importante para conter a vassoura de bruxa é estudar as interações da enzima lanosterol 14α-demethylase (CYP51) de Moniliophthora com compostos azólicos. Estes compostos bloqueiam a síntese de ergosterol e, consequentemente, o crescimento fúngico pela ligação entre o átomo de ferro do cofactor dessa enzima e o átomo de nitrogênio do grupo azol. No entanto, não há um estudo sistemático sobre a interação destes compostos com a enzima lanosterol 14α-demetilase deste patógeno. Neste trabalho, um modelo da enzima lanosterol 14α-demetilase do M. perniciosa foi criado por técnicas de modelagem comparativa. Em seguida, o arranjo espacial dos resíduos que formam o sítio catalítico da enzima foi identificado. Os resultados mostram que o modelo construído pode ser empregado em estudos de ancoragem molecular e de novo design. Palavras-chave:Moniliophthora perniciosa, modelagem molecular, compostos azóis, CYP51.

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Crystal structure of auxin-binding protein 1 in complex with auxin

Cited by 147 publications

References 45 publications

AUXIN BINDING PROTEIN1: The Outsider

AUXIN BINDING PROTEIN1: The Outsider

The polyketide cyclase RemF from Streptomyces resistomycificus contains an unusual octahedral zinc binding site

Estudos de Modelagem Comparativa da lanosterol 14-alfa demetilase de Moniliophthora perniciosa

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