Crystal structure of MBP-PigG fusion protein and the essential function of PigG in the prodigiosin biosynthetic pathway in Serratia marcescens FS14

Zhang, Fan; Wei, Qiaoe; Tong, Huan; Xu, Dongqing; Wang, Weiwu; Ran, Tingting

doi:10.1016/j.ijbiomac.2017.02.088

Cited by 8 publications

(11 citation statements)

References 36 publications

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“…In Figure 2, we present two pieces of evidence that seem to indicate that beyond the in silico analysis and protein modeling, the extracellular domain of JAMs is composed of high βsheet structures. The crystal structure of MBP [34], as well as CD [35] data, found in the literature, and performed at 21 °C has been reported to have an α-helix content of 36%, and a β-sheet content of 17%. We used these values to compare our results.…”

Section: Determination Of Conserved Secondary Structures By Circular mentioning

confidence: 90%

Molecular Characterization of the Extracellular Domain of Human Junctional Adhesion Proteins

Mendoza

Nagidi

Mizrachi

2021

IJMS

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The junction adhesion molecule (JAM) family of proteins play central roles in the tight junction (TJ) structure and function. In contrast to claudins (CLDN) and occludin (OCLN), the other membrane proteins of the TJ, whose structure is that of a 4α-helix bundle, JAMs are members of the immunoglobulin superfamily. The JAM family is composed of four members: A, B, C and 4. The crystal structure of the extracellular domain of JAM-A continues to be used as a template to model the secondary and tertiary structure of the other members of the family. In this article, we have expressed the extracellular domains of JAMs fused with maltose-binding protein (MBP). This strategy enabled the work presented here, since JAM-B, JAM-C and JAM4 are more difficult targets due to their more hydrophobic nature. Our results indicate that each member of the JAM family has a unique tertiary structure in spite of having similar secondary structures. Surface plasmon resonance (SPR) revealed that heterotypic interactions among JAM family members can be greatly favored compared to homotypic interactions. We employ the well characterized epithelial cadherin (E-CAD) as a means to evaluate the adhesive properties of JAMs. We present strong evidence that suggests that homotypic or heterotypic interactions among JAMs are stronger than that of E-CADs.

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Section: Determination Of Conserved Secondary Structures By Circular mentioning

confidence: 90%

Molecular Characterization of the Extracellular Domain of Human Junctional Adhesion Proteins

Mendoza

Nagidi

Mizrachi

2021

IJMS

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“…The restriction sites of endonucleases Nde I and Xho I in baeS (residues 34–160) (bases underlined) were created by the primers. The PCR product was digested and ligated into the Nde I and Xho I sites of pET‐28a containing the gene encoding MBP domains (1–374) . The sequence‐verified plasmid was then transformed into E. coli C43 (DE3) cells for protein expression.…”

Section: Methodsmentioning

confidence: 99%

“…The PCR product was digested and ligated into the NdeI and XhoI sites of pET-28a containing the gene encoding MBP domains (1-374). 22 The sequence-verified plasmid was then transformed into E. coli C43 (DE3) cells for protein expression. This fusion protein is referred to as MBP-BaeS .…”

Section: Cloning Overproduction and Purificationmentioning

confidence: 99%

Crystal structure of the sensor domain of BaeS from Serratia marcescens FS14

Qiu

Jia

et al. 2017

Proteins

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The sensor histidine kinases of two-component signal-transduction systems (TCSs) are essential for bacteria to adapt to variable environmental conditions. The two-component regulatory system BaeS/R increases multidrug and metal resistance in Salmonella and Escherichia coli. In this study, we report the X-ray structure of the periplasmic sensor domain of BaeS from Serratia marcescens FS14. The BaeS sensor domain (34-160) adopts a mixed α/β-fold containing a central four-stranded antiparallel β-sheet flanked by a long N-terminal α-helix and additional loops and a short C-terminal α-helix on each side. Structural comparisons revealed that it belongs to the PDC family with a remarkable difference in the orientation of the helix α2. In the BaeS sensor domain, this helix is situated perpendicular to the long helix α1 and holds helix α1 in the middle with the beta sheet, whereas in other PDC domains, helix α2 is parallel to helix α1. Because the helices α1 and α2 is involved in the dimeric interface, this difference implies that BaeS uses a different dimeric interface compared with other PDC domains. Proteins 2017; 85:1784-1790. © 2017 Wiley Periodicals, Inc.

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“…Despite extensive research into the biosynthetic pathways for prodigiosin, so far the structures of only two proteins, PigG and PigE, have been determined . Recently, the structure of AnaB, a homologue with 41 % sequence identity to that of PigA, which catalyzes proline oxidization in anatoxin biosynthesis, has been solved .…”

Section: Introductionmentioning

confidence: 99%

Crystal Structure of PigA: A Prolyl Thioester‐Oxidizing Enzyme in Prodigiosin Biosynthesis

Lee

Chen

et al. 2018

ChemBioChem

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Prodigiosin is an intensely red pigment comprising three pyrroles. The biosynthetic pathway includes a two-step proline oxidation catalyzed by phosphatidylinositol N-acetylglucosaminyltransferase subunit A (PigA), with flavin adenine dinucleotide (FAD) as its cofactor. The enzyme is crystallized in the apo form and in complex with FAD and proline. As an acyl coenzyme A dehydrogenase (ACAD) family member, the protein folds into a β-sheet flanked by two α-helical domains. PigA forms a tetramer, which is consistent with analytical ultracentrifugation results. FAD binds to PigA in a similar way to that in the other enzymes of the ACAD family. The variable conformations of loop β4-β5 and helix αG correlate well with the structural flexibility required for substrate entrance to the Re side of FAD. Modeling with PigG, the acyl carrier protein, suggests a reasonable mode of interaction with PigA. The structure helps to explain the proline oxidation mechanism, in which Glu244 plays a central role by abstracting the substrate protons. It also reveals a plausible pocket for oxygen binding to the Si side of FAD.

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Crystal structure of MBP-PigG fusion protein and the essential function of PigG in the prodigiosin biosynthetic pathway in Serratia marcescens FS14

Cited by 8 publications

References 36 publications

Molecular Characterization of the Extracellular Domain of Human Junctional Adhesion Proteins

Molecular Characterization of the Extracellular Domain of Human Junctional Adhesion Proteins

Crystal structure of the sensor domain of BaeS from Serratia marcescens FS14

Crystal Structure of PigA: A Prolyl Thioester‐Oxidizing Enzyme in Prodigiosin Biosynthesis

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