Sandbox GGC1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (19:13, 28 April 2021) (edit) (undo)
 
(114 intermediate revisions not shown.)
Line 1: Line 1:
-
Crystal Structure of yeast nitronate monooxygenase from ''Cyberlindera saturnas''
+
==Kinesin Motor Domain==
-
<StructureSection load='6BKA' size='340' side='right' caption='Caption for this structure' scene=''>
+
<StructureSection load='1bg2' size='340' side='right' caption='Kinesin Protein' scene=''>
-
<scene name='75/752263/Alpha_beta_sheets/1'>This view</scene> shows the alpha helixes and beta pleaded sheets of nitronate monooxygenase.
+
Kinesin is an ATP-dependent motor protein responsible for the transportation of cargo. It is a heterotetramer composed of light and heavy chains.
-
Nitronate Monooxygenase (NMO) is an FMN-dependent (flavin mononucleotide) enzyme that oxidizes the neurotoxin propionate 3-nitronate (P3N). FMN is produced from riboflavin or Vitamin B2 by riboflavin kinase and can function as a prosthetic group for NADH dehydrogenase <ref>Huerta C, Borek D, Machius M, Grishin NV, Zhang H. Structure and Mechanism of a Eukaryotic FMN Adenylyltransferase. Journal of molecular biology. 2009;389(2):388-400. doi:10.1016/j.jmb.2009.04.022.</ref>. NMO is widely known as the best system for P3N detoxification in many different organisms.
+
 +
== '''Function''' ==
 +
* Moving cargo usually from the center of the cell to the margins <br/>
 +
* Involved in cell replication and axonal signaling
 +
== '''Disease''' ==
 +
*Charcot Marie Tooth (CMT): Charcot Marie Tooth is one of many diseases that affect the peripheral nervous system. Individuals may suffer physical disabilities due to weakness in transmission of signals firing from the central nervous system
-
== Function ==
 
-
NMOs are FMN-dependent enzymes that can quickly and efficiently catalyze the oxidation of P3N. They can also oxidize alkyl nitronates but with lower catalytic efficiency in comparison to P3N.<ref> Francis K, Nishino SF, Spain JC, Gadda G. A novel activity for fungal nitronate monooxygenase: detoxification of the metabolic inhibitor propionate-3-nitronate. Arch Biochem Biophys. 2012;521(1–2):84–89.</ref><ref>Gadda G, Francis K. Nitronate monooxygenase, a model for anionic flavin semiquinone intermediates in oxidative catalysis. Arch Bio-chem Biophys. 2010;493(1):53–61.</ref> Recent structural studies suggest there are two classes of NMOs, Class I and Class II.<ref>Salvi F, Agniswamy J, Yuan H, et al. The combined structural and kinetic characterization of a bacterial nitronate monooxygenase from Pseudomonas aeruginosa PAO1 establishes NMO class I and II.J Biol Chem. 2014;289(34):23764–23775.</ref> Class I NMOs
 
-
== Disease ==
+
== '''Structural highlights''' ==
-
P3N can be considered a toxic compound that is commonly found in legumes, fungi, and leaf beetles. During hydrolysis, P3N is released from esters and acts as an irreversible inhibitor of mitochondrial succinate dehydrogenase. <ref>Hipkin CR, Simpson DJ, Wainwright SJ, Salem MA. Nitrification by plants that also fix nitrogen. Nature. 2004;430(6995):98–101</ref> Succinate dehydrogenase is a key enzyme in the Kreb's cycle and the electron transport chain for oxidative phosphorylation. Because this is inhibited, it can lead to a variety of neurological disorders and can even cause death. <ref>Francis K, Smitherman C, Nishino SF, Spain JC, Gadda G. The bio-chemistry of the metabolic poison propionate 3-nitronate and its conjugate acid, 3-nitropropionate. IUBMB Life. 2013;65(9):759–768.</ref>
+
 +
;Scene #1: Kinesin structure is composed of eight anti-parallel Beta sheets and three alpha helices on opposite sides <scene name='75/752263/Alpha_beta_sheets/5'> Alpha-beta structure </scene>
-
== Structural highlights ==
+
;Scene #2: This is the ATP binding site. Upon the binding of phosphate to ADP, ATP is formed giving Kinesin the energy needed to move the cargo one step a head to its destination <scene name='75/752263/Atp_binding_site/5'> ATP-binding site </scene>
 +
 
 +
;Scene #3: This is the Microtubule-binding site, where Kinesin binds to microtubules for stability <scene name='75/752263/Mt-binding_site/1'> MT-binding site </scene>
 +
 
 +
;Scene #4: some patients with CMT show mutation in the p-loop. A missense mutation results in a leucine in place of glutamine affecting signal transmission <scene name='75/752263/Cmt/1'> CMT </scene>
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
Line 19: Line 25:
</StructureSection>
</StructureSection>
== References ==
== References ==
-
 
+
#file:///C:/Users/Muna/Desktop/Spring%202021/Advanced%20Biochem/pcbi.1003329.pdf
 +
#https://www.ncbi.nlm.nih.gov/books/NBK22572/#:~:text=Kinesins%20moving%20along%20microtubules%20usually,surfaces%20of%20some%20eukaryotic%20cells.
 +
#https://www.ninds.nih.gov/Disorders/Patient-Caregiver-Education/Fact-Sheets/Charcot-Marie-Tooth-Disease-Fact-Sheet
<references/>
<references/>

Current revision

Kinesin Motor Domain

Kinesin Protein

Drag the structure with the mouse to rotate

References

  1. file:///C:/Users/Muna/Desktop/Spring%202021/Advanced%20Biochem/pcbi.1003329.pdf
  2. https://www.ncbi.nlm.nih.gov/books/NBK22572/#:~:text=Kinesins%20moving%20along%20microtubules%20usually,surfaces%20of%20some%20eukaryotic%20cells.
  3. https://www.ninds.nih.gov/Disorders/Patient-Caregiver-Education/Fact-Sheets/Charcot-Marie-Tooth-Disease-Fact-Sheet
Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_GGC1"
Personal tools