We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2bpl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:14, 24 April 2013) (edit) (undo)
(Redirecting to 4amv)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2bpl.gif|left|200px]]
+
#REDIRECT [[4amv]] This PDB entry is obsolete and replaced by 4amv
-
 
+
-
{{Structure
+
-
|PDB= 2bpl |SIZE=350|CAPTION= <scene name='initialview01'>2bpl</scene>, resolution 2.05&Aring;
+
-
|SITE= <scene name='pdbsite=AC1:F6r+Binding+Site+For+Chain+B'>AC1</scene>
+
-
|LIGAND= <scene name='pdbligand=F6R:FRUCTOSE -6-PHOSPHATE'>F6R</scene>
+
-
|ACTIVITY= [http://en.wikipedia.org/wiki/Glutamine--fructose-6-phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16]
+
-
|GENE=
+
-
}}
+
-
 
+
-
'''E.COLI GLUCOSAMINE-6P SYNTHASE IN COMPLEX WITH FRUCTOSE-6P'''
+
-
 
+
-
 
+
-
==Overview==
+
-
Glucosamine-6P synthase catalyzes the synthesis of glucosamine-6P from fructose-6P and glutamine and uses a channel to transfer ammonia from its glutaminase to its synthase active site. X-ray structures of glucosamine-6P synthase have been determined at 2.05 Angstroms resolution in the presence of fructose-6P and at 2.35 Angstroms resolution in the presence of fructose-6P and 6-diazo-5-oxo-L-norleucine, a glutamine affinity analog that covalently modifies the N-terminal catalytic cysteine, therefore mimicking the gamma-glutamyl-thioester intermediate formed during hydrolysis of glutamine. The fixation of the glutamine analog activates the enzyme through several major structural changes: 1) the closure of a loop to shield the glutaminase site accompanied by significant domain hinging, 2) the activation of catalytic residues involved in glutamine hydrolysis, i.e. the alpha-amino group of Cys-1 and Asn-98 that is positioned to form the oxyanion hole, and 3) a 75 degrees rotation of the Trp-74 indole group that opens the ammonia channel.
+
-
 
+
-
==About this Structure==
+
-
2BPL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BPL OCA].
+
-
 
+
-
==Reference==
+
-
Glutamine binding opens the ammonia channel and activates glucosamine-6P synthase., Mouilleron S, Badet-Denisot MA, Golinelli-Pimpaneau B, J Biol Chem. 2006 Feb 17;281(7):4404-12. Epub 2005 Dec 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16339762 16339762]
+
-
[[Category: Escherichia coli]]
+
-
[[Category: Glutamine--fructose-6-phosphate transaminase (isomerizing)]]
+
-
[[Category: Single protein]]
+
-
[[Category: Golinelli-Pimpaneau, B.]]
+
-
[[Category: Mouilleron, S.]]
+
-
[[Category: F6R]]
+
-
[[Category: amidotransferase]]
+
-
[[Category: ammonia channeling]]
+
-
[[Category: fructose 6-phosphate]]
+
-
[[Category: glucosamine 6-phosphate synthase]]
+
-
[[Category: glutamine amidotransferase]]
+
-
[[Category: n terminal nucleophile]]
+
-
[[Category: transferase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:04:58 2008''
+

Current revision

  1. REDIRECT 4amv This PDB entry is obsolete and replaced by 4amv

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bpl"
Personal tools