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Analysis of institutional authors

Santamaria-Hernando, SarayAuthor

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June 9, 2019
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Identification of a Novel Calcium Binding Motif Based on the Detection of Sequence Insertions in the Animal Peroxidase Domain of Bacterial Proteins

Publicated to: Plos One. 7 (7): e40698- - 2012-07-13 7(7), DOI: 10.1371/journal.pone.0040698

Authors:

Santamaria-Hernando, Saray; Krell, Tino; Ramos-Gonzalez, Maria-Isabel;
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Affiliations

Estac Expt Zaidin Consejo Super Invest CSIC, Environm Protect Dept, Granada, Spain - Author

Abstract

Proteins of the animal heme peroxidase (ANP) superfamily differ greatly in size since they have either one or two catalytic domains that match profile PS50292. The orf PP_2561 of Pseudomonas putida KT2440 that we have called PepA encodes a two-domain ANP. The alignment of these domains with those of PepA homologues revealed a variable number of insertions with the consensus G-x-D-G-x-x-[GN]-[TN]-x-D-D. This motif has also been detected in the structure of pseudopilin (pdb 3G20), where it was found to be involved in Ca2+ coordination although a sequence analysis did not reveal the presence of any known calcium binding motifs in this protein. Isothermal titration calorimetry revealed that a peptide containing this consensus motif bound specifically calcium ions with affinities ranging between 33-79 mu M depending on the pH. Microcalorimetric titrations of the purified N-terminal ANP-like domain of PepA revealed Ca2+ binding with a K-D of 12 mu M and stoichiometry of 1.25 calcium ions per protein monomer. This domain exhibited peroxidase activity after its reconstitution with heme. These data led to the definition of a novel calcium binding motif that we have termed PERCAL and which was abundantly present in animal peroxidase-like domains of bacterial proteins. Bacterial heme peroxidases thus possess two different types of calcium binding motifs, namely PERCAL and the related hemolysin type calcium binding motif, with the latter being located outside the catalytic domains and in their C-terminal end. A phylogenetic tree of ANP-like catalytic domains of bacterial proteins with PERCAL motifs, including single domain peroxidases, was divided into two major clusters, representing domains with and without PERCAL motif containing insertions. We have verified that the recently reported classification of bacterial heme peroxidases in two families (cd09819 and cd09821) is unrelated to these insertions. Sequences matching PERCAL were detected in all kingdoms of life.
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Keywords

Escherichia-coliInactivationLignin peroxidaseMn(ii) oxidationNodulationPseudomonas-putida

Quality index

Bibliometric impact. Analysis of the contribution and dissemination channel

The work has been published in the journal Plos One due to its progression and the good impact it has achieved in recent years, according to the agency WoS (JCR), it has become a reference in its field. In the year of publication of the work, 2012, it was in position 7/56, thus managing to position itself as a Q1 (Primer Cuartil), in the category Multidisciplinary Sciences.

Independientemente del impacto esperado determinado por el canal de difusión, es importante destacar el impacto real observado de la propia aportación.

Según las diferentes agencias de indexación, el número de citas acumuladas por esta publicación hasta la fecha 2025-12-21:

  • WoS: 12
  • Scopus: 14
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Impact and social visibility

From the perspective of influence or social adoption, and based on metrics associated with mentions and interactions provided by agencies specializing in calculating the so-called "Alternative or Social Metrics," we can highlight as of 2025-12-21:

  • The use of this contribution in bookmarks, code forks, additions to favorite lists for recurrent reading, as well as general views, indicates that someone is using the publication as a basis for their current work. This may be a notable indicator of future more formal and academic citations. This claim is supported by the result of the "Capture" indicator, which yields a total of: 37 (PlumX).

It is essential to present evidence supporting full alignment with institutional principles and guidelines on Open Science and the Conservation and Dissemination of Intellectual Heritage. A clear example of this is:

  • The work has been submitted to a journal whose editorial policy allows open Open Access publication.
  • Assignment of a Handle/URN as an identifier within the deposit in the Institutional Repository: https://oa.upm.es/86221/

As a result of the publication of the work in the institutional repository, statistical usage data has been obtained that reflects its impact. In terms of dissemination, we can state that, as of

  • Views: 119
  • Downloads: 21
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Leadership analysis of institutional authors

There is a significant leadership presence as some of the institution’s authors appear as the first or last signer, detailed as follows: First Author (SANTAMARIA HERNANDO, SARAY) .

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Awards linked to the item

S.S.H. was granted with a predoctoral fellowship from Junta de Andalucia. This work was supported by grants P07-CVI-03156 from Junta de Andalucia http://www.juntadeandalucia.es/organismos/economiainnovacionyciencia/ and EDFR, and BFU2010-17946 from the Plan Nacional de I+D+I http://www.idi.mineco.gob.es/portal/site/MICINN/ and EDFR to M.I.R.G. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
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