3qrx

From Proteopedia

(Difference between revisions)

Revision as of 06:21, 8 June 2022

Chlamydomonas reinhardtii centrin bound to melittin

Structural highlights

3qrx is a 2 chain structure with sequence from Chlre. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	VFL2, CHLREDRAFT_159554 (CHLRE)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MEL_APIME] Melittin: Main toxin of bee venom with strong hemolytic activity. Forms a pore in the cell membrane by inserting into lipid bilayers in an alpha-helical conformation and has multiple effects, probably, as a result of its interaction with negatively charged phospholipids. It inhibits well known transport pumps such as the Na(+)-K(+)-ATPase and the H(+)-K(+)-ATPase. It increases the permeability of cell membranes to ions, particularly Na(+) and indirectly Ca(2+), because of the Na(+)-Ca(2+)-exchange. It acts synergistically with phospholipase A2.^[1] Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.^[2]

Publication Abstract from PubMed

Centrin is a calcium binding protein (CaBP) belonging to the EF-hand superfamily. As with other proteins within this family, centrin is a calcium sensor with multiple biological target proteins. We chose to study Chlamydomonas reinhardtii centrin (Crcen) and its interaction with melittin (MLT) as a model for CaBP complexes due to its amphipathic properties. Our goal was to determine the molecular interactions that lead to centrin-MLT complex formation, their relative stability, and the conformational changes associated with the interaction, when compared to the single components. For this, we determined the thermodynamic parameters that define Crcen-MLT complex formation. Two-dimensional infrared (2D IR) correlation spectroscopy were used to study the amide I', I'*, and side chain bands for (13) C-Crcen, MLT, and the (13) C-Crcen-MLT complex. This approach resulted in the determination of MLT's increased helicity, while centrin was stabilized within the complex. Herein we provide the first complete molecular description of centrin-MLT complex formation and the dissociation process. Also, discussed is the first structure of a CaBP-MLT complex by X-ray crystallography, which shows that MLT has a different binding orientation than previously characterized centrin-bound peptides. Finally, all of the experimental results presented herein are consistent with centrin maintaining an extended conformation while interacting with MLT. The molecular implications of these results are: (1) the recognition of hydrophobic contacts as requirements for initial binding, (2) minimum electrostatic interactions within the C-terminal end of the peptide, and (3) van der Waals interactions within MLTs N-terminal end are required for complex formation. Proteins 2011; (c) 2011 Wiley-Liss, Inc.

The structure, molecular dynamics, and energetics of centrin-melittin complex.,Sosa Ldel V, Alfaro E, Santiago J, Narvaez D, Rosado MC, Rodriguez A, Gomez AM, Schreiter ER, Pastrana-Rios B Proteins. 2011 Nov;79(11):3132-43. doi: 10.1002/prot.23142. Epub 2011 Aug, 30. PMID:21989934^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sciani JM, Marques-Porto R, Lourenco Junior A, Orsi Rde O, Ferreira Junior RS, Barraviera B, Pimenta DC. Identification of a novel melittin isoform from Africanized Apis mellifera venom. Peptides. 2010 Aug;31(8):1473-9. doi: 10.1016/j.peptides.2010.05.001. Epub 2010, May 21. PMID:20472009 doi:http://dx.doi.org/10.1016/j.peptides.2010.05.001
↑ Sciani JM, Marques-Porto R, Lourenco Junior A, Orsi Rde O, Ferreira Junior RS, Barraviera B, Pimenta DC. Identification of a novel melittin isoform from Africanized Apis mellifera venom. Peptides. 2010 Aug;31(8):1473-9. doi: 10.1016/j.peptides.2010.05.001. Epub 2010, May 21. PMID:20472009 doi:http://dx.doi.org/10.1016/j.peptides.2010.05.001
↑ Sosa Ldel V, Alfaro E, Santiago J, Narvaez D, Rosado MC, Rodriguez A, Gomez AM, Schreiter ER, Pastrana-Rios B. The structure, molecular dynamics, and energetics of centrin-melittin complex. Proteins. 2011 Nov;79(11):3132-43. doi: 10.1002/prot.23142. Epub 2011 Aug, 30. PMID:21989934 doi:10.1002/prot.23142

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3qrx"

@@ Line 1: / Line 1: @@
 ==Chlamydomonas reinhardtii centrin bound to melittin==
-<StructureSection load='3qrx' size='340' side='right' caption='[[3qrx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='3qrx' size='340' side='right'caption='[[3qrx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3qrx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlre Chlre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QRX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QRX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3qrx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlre Chlre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QRX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VFL2, CHLREDRAFT_159554 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VFL2, CHLREDRAFT_159554 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qrx OCA], [http://pdbe.org/3qrx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qrx RCSB], [http://www.ebi.ac.uk/pdbsum/3qrx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qrx ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qrx OCA], [https://pdbe.org/3qrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qrx RCSB], [https://www.ebi.ac.uk/pdbsum/3qrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qrx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MEL_APIME MEL_APIME]] Melittin: Main toxin of bee venom with strong hemolytic activity. Forms a pore in the cell membrane by inserting into lipid bilayers in an alpha-helical conformation and has multiple effects, probably, as a result of its interaction with negatively charged phospholipids. It inhibits well known transport pumps such as the Na(+)-K(+)-ATPase and the H(+)-K(+)-ATPase. It increases the permeability of cell membranes to ions, particularly Na(+) and indirectly Ca(2+), because of the Na(+)-Ca(2+)-exchange. It acts synergistically with phospholipase A2.<ref>PMID:20472009</ref>   Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.<ref>PMID:20472009</ref>
+[[https://www.uniprot.org/uniprot/MEL_APIME MEL_APIME]] Melittin: Main toxin of bee venom with strong hemolytic activity. Forms a pore in the cell membrane by inserting into lipid bilayers in an alpha-helical conformation and has multiple effects, probably, as a result of its interaction with negatively charged phospholipids. It inhibits well known transport pumps such as the Na(+)-K(+)-ATPase and the H(+)-K(+)-ATPase. It increases the permeability of cell membranes to ions, particularly Na(+) and indirectly Ca(2+), because of the Na(+)-Ca(2+)-exchange. It acts synergistically with phospholipase A2.<ref>PMID:20472009</ref>   Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.<ref>PMID:20472009</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 24: @@
 </StructureSection>
 [[Category: Chlre]]
+[[Category: Large Structures]]
 [[Category: Schreiter, E R]]
 [[Category: Calcium binding]]

3qrx

From Proteopedia

Revision as of 06:21, 8 June 2022

Chlamydomonas reinhardtii centrin bound to melittin

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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