1hze

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:43, 3 April 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1hze.jpg|left|200px]]
 
-
{{Structure
+
==SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOFLAVIN SYNTHASE FROM E. COLI==
-
|PDB= 1hze |SIZE=350|CAPTION= <scene name='initialview01'>1hze</scene>
+
<StructureSection load='1hze' size='340' side='right'caption='[[1hze]]' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=RBF:RIBOFLAVINE'>RBF</scene>
+
<table><tr><td colspan='2'>[[1hze]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HZE FirstGlance]. <br>
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Riboflavin_synthase Riboflavin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.9 2.5.1.9] </span>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RBF:RIBOFLAVIN'>RBF</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hze OCA], [https://pdbe.org/1hze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hze RCSB], [https://www.ebi.ac.uk/pdbsum/1hze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hze ProSAT]</span></td></tr>
-
|RELATEDENTRY=
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hze OCA], [http://www.ebi.ac.uk/pdbsum/1hze PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hze RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/RISA_ECOLI RISA_ECOLI] Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.
-
 
+
== Evolutionary Conservation ==
-
'''SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOFLAVIN SYNTHASE FROM E. COLI'''
+
[[Image:Consurf_key_small.gif|200px|right]]
-
 
+
Check<jmol>
-
 
+
<jmolCheckbox>
-
==Overview==
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hz/1hze_consurf.spt"</scriptWhenChecked>
-
The structure of the amino-terminal domain of Escherichia coli riboflavin synthase (RiSy) has been determined by NMR spectroscopy with riboflavin as a bound ligand. RiSy is functional as a 75 kDa homotrimer, each subunit of which consists of two domains which share very similar sequences and structures. The N-terminal domain (RiSy-N; 97 residues) forms a 20 kDa homodimer in solution which binds riboflavin with high affinity. The structure features a six-stranded antiparallel beta-barrel with a Greek-key fold, both ends of which are closed by an alpha-helix. One riboflavin molecule is bound per monomer in a site at one end of the barrel which is comprised of elements of both monomers. The structure and ligand binding are similar to that of the FAD binding domains of ferrodoxin reductase family proteins. The structure provides insights into the structure of the whole enzyme, the organisation of the functional trimer and the mechanism of riboflavin synthesis. C48 from the N-terminal domain is identified as the free cysteine implicated in a nucleophilic role in the synthesis mechanism, while H102 from the C-terminal domains is also likely to play a key role. Both are invariant in all known riboflavin synthase sequences.
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
 
+
<text>to colour the structure by Evolutionary Conservation</text>
-
==About this Structure==
+
</jmolCheckbox>
-
1HZE 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=1HZE OCA].
+
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hze ConSurf].
-
 
+
<div style="clear:both"></div>
-
==Reference==
+
__TOC__
-
The solution structure of the N-terminal domain of riboflavin synthase., Truffault V, Coles M, Diercks T, Abelmann K, Eberhardt S, Luttgen H, Bacher A, Kessler H, J Mol Biol. 2001 Jun 15;309(4):949-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11399071 11399071]
+
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Riboflavin synthase]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Abelmann K]]
-
[[Category: Abelmann, K.]]
+
[[Category: Bacher A]]
-
[[Category: Bacher, A.]]
+
[[Category: Coles M]]
-
[[Category: Coles, M.]]
+
[[Category: Diercks T]]
-
[[Category: Diercks, T.]]
+
[[Category: Eberhardt S]]
-
[[Category: Eberhardt, S.]]
+
[[Category: Kessler H]]
-
[[Category: Kessler, H.]]
+
[[Category: Luettgen H]]
-
[[Category: Luettgen, H.]]
+
[[Category: Truffault V]]
-
[[Category: Truffault, V.]]
+
-
[[Category: greek-key-barrel]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:12:26 2008''
+

Current revision

SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOFLAVIN SYNTHASE FROM E. COLI

PDB ID 1hze

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools