Functional analysis of 2qgn: Difference between revisions

From MDWiki
Jump to navigationJump to search
No edit summary
No edit summary
 
(34 intermediate revisions by 3 users not shown)
Line 1: Line 1:
Transferases are enzymes which transfer a group from a donor molecule to an acceptor molecule. As the name suggest, tRNA-IPT adds isopentenyl group to the adenine residue on tRNA molecules specifically to tRNA, whose anticodon binds to the codon encoded with uridine. Below is the reaction catalysed by tRNA isopentenyltransferase.
'''Function from its name'''


Isopentenyl diphosphate + tRNA <=> diphosphate + tRNA containing 6-isopentenyladenosine
[[Image:reaction1.png|framed|center|none]]
                                               
reaction taken from http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.8


tRNA molecules with modified adenine specifically at position 37 are known as cytokinins.This modified adenine is found next to the anticodon that binds to the codon encoding for uridine.
[[How the enzyme act on tRNA| Next]]
This detailed and precise adenine modification is important in maintaining correct framework and the subsequent translation pathway.
 
Cytokinins are involved in several biochemical and cellular processes such as cell division and growth, both in plants and animals. They can exist in two forms; the tRNA-free and the tRNA-bound form, through addition of adenine to tRNA or AMP acceptor molecules.
 
Molecular function and biological processes of this enzyme was obtained from the ProKnow server.
Molecular function of this enzyme is ATP binding. This means that the enzyme interacts selectively with ATP at the 5'end and acts as a universally important coenzyme and enzyme regulator.
On the other hand, the biological process of this enzyme is tRNA modification. This involves the covalent alteration of one or more nucleotides within the tRNA, thus leading to a change in the properties of the tRNA.
 
==Localisation of Expression==
[[Image:Mouse gene atlas.png]]
 
 
[[Image:Human geneAtlas.png]]
 
 
using the motif search, The C2-H2 Zinc finger motif found in tRNA-IPT also contributes to the enzyme's function. This motif is commonly found in nucleic acid-binding proteins and is composed of 25 to 30 amino acid residues.
 
Motif ZINC_FINGER_C2H2_1 in your sequence
 
Prosite ID:
ZINC_FINGER_C2H2_1 (PS00028)
 
Description:
Zinc finger C2H2 type domain signature.
 
Pattern:
C-x(2,4)-C-x(3)-[LIVMFYWC]-x(8)-H-x(3,5)-H.
 
Appearance:
Position Found Motif
396..418 CDLCDRIIIGDREWAAHIKSKSH
 
Sequence:
MASVAAARAVPVGSGLRGLQRTLPLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVE
GLDIITNKVSAQEQRICRHHMISFVDPLVTNYTVVDFRNRATALIEDIFARDKIPIVVGG
TNYYIESLLWKVLVNTKPQEMGTEKVIDRKVELEKEDGLVLHKRLSQVDPEMAAKLHPHD
KRKVARSLQVFEETGISHSEFLHRQHTEEGGGPLGGPLKFSNPCILWLHADQAVLDERLD
KRVDDMLAAGLLEELRDFHRRYNQKNVSENSQDYQHGIFQSIGFKEFHEYLITEGKCTLE
TSNQLLKKGIEALKQVTKRYARKQNRWVKNRFLSRPGPIVPPVYGLEVSDVSKWEESVLE
PALEIVQSFIQGHKPTATPIKMPYNEAENKRSYHLCDLCDRIIIGDREWAAHIKSKSHLN
QLKKRRRLDSDAVNTIESQSVSPDHNKEPKEKGSPGQNDQELKCSV
 
 
 
 
 
A schematic representation of a zinc finger domain is shown below:
                                x  x
                              x      x
                              x        x
                              x        x
                              x        x
                              x        x
                              C      H
                            x  \  /  x
                            x    Zn    x
                            x  /    \  x
                              C      H
                      x x x x x        x x x x x
 
 
http://ca.expasy.org/cgi-bin/nicedoc.pl?PDOC00028
 
GENOMIC CONTEXT
In bacteria, the gene encoding this enzyme is known as miaA while the human and S. cerevisaea is TRIT1 and mod5 respectively. Although gene name differ in different organisms, they all synthesize enzyme of the same function.
 
'''Sequence Motif'''
 
[[Image:motif.jpg]]
 
 
'''Molecular Function'''
 
 
 
[[Image:PROKNOW2- molecular function.png]]
 
'''Biological Process'''
 
 
 
[[Image:PROKNOW-biological process.png]]

Latest revision as of 14:28, 9 June 2008

Function from its name

Reaction1.png

Next