2i56

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2i56.jpg|left|200px]]<br /><applet load="2i56" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2i56.jpg|left|200px]]
-
caption="2i56, resolution 1.97&Aring;" />
+
 
-
'''Crystal structure of L-Rhamnose Isomerase from Pseudomonas stutzeri with L-Rhamnose'''<br />
+
{{Structure
 +
|PDB= 2i56 |SIZE=350|CAPTION= <scene name='initialview01'>2i56</scene>, resolution 1.97&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=RNS:L-RHAMNOSE'>RNS</scene> and <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/L-rhamnose_isomerase L-rhamnose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.14 5.3.1.14]
 +
|GENE=
 +
}}
 +
 
 +
'''Crystal structure of L-Rhamnose Isomerase from Pseudomonas stutzeri with L-Rhamnose'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2I56 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri] with <scene name='pdbligand=RNS:'>RNS</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/L-rhamnose_isomerase L-rhamnose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.14 5.3.1.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I56 OCA].
+
2I56 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I56 OCA].
==Reference==
==Reference==
-
The structures of L-rhamnose isomerase from Pseudomonas stutzeri in complexes with L-rhamnose and D-allose provide insights into broad substrate specificity., Yoshida H, Yamada M, Ohyama Y, Takada G, Izumori K, Kamitori S, J Mol Biol. 2007 Feb 2;365(5):1505-16. Epub 2006 Nov 6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17141803 17141803]
+
The structures of L-rhamnose isomerase from Pseudomonas stutzeri in complexes with L-rhamnose and D-allose provide insights into broad substrate specificity., Yoshida H, Yamada M, Ohyama Y, Takada G, Izumori K, Kamitori S, J Mol Biol. 2007 Feb 2;365(5):1505-16. Epub 2006 Nov 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17141803 17141803]
[[Category: L-rhamnose isomerase]]
[[Category: L-rhamnose isomerase]]
[[Category: Pseudomonas stutzeri]]
[[Category: Pseudomonas stutzeri]]
Line 26: Line 35:
[[Category: tim barrel]]
[[Category: tim barrel]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:49:18 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:25:32 2008''

Revision as of 15:25, 20 March 2008


PDB ID 2i56

Drag the structure with the mouse to rotate
, resolution 1.97Å
Ligands: and
Activity: L-rhamnose isomerase, with EC number 5.3.1.14
Coordinates: save as pdb, mmCIF, xml



Crystal structure of L-Rhamnose Isomerase from Pseudomonas stutzeri with L-Rhamnose


Overview

Pseudomonas stutzeri L-rhamnose isomerase (P. stutzeri L-RhI) can efficiently catalyze the isomerization between various aldoses and ketoses, showing a broad substrate specificity compared to L-RhI from Escherichia coli (E. coli L-RhI). To understand the relationship between structure and substrate specificity, the crystal structures of P. stutzeri L-RhI alone and in complexes with L-rhamnose and D-allose which has different configurations of C4 and C5 from L-rhamnose, were determined at a resolution of 2.0 A, 1.97 A, and 1.97 A, respectively. P. stutzeri L-RhI has a large domain with a (beta/alpha)(8) barrel fold and an additional small domain composed of seven alpha-helices, forming a homo tetramer, as found in E. coli L-RhI and D-xylose isomerases (D-XIs) from various microorganisms. The beta1-alpha1 loop (Gly60-Arg76) of P. stutzeri L-RhI is involved in the substrate binding of a neighbouring molecule, as found in D-XIs, while in E. coli L-RhI, the corresponding beta1-alpha1 loop is extended (Asp52-Arg78) and covers the substrate-binding site of the same molecule. The complex structures of P. stutzeri L-RhI with L-rhamnose and D-allose show that both substrates are nicely fitted to the substrate-binding site. The part of the substrate-binding site interacting with the substrate at the 1, 2, and 3 positions is equivalent to E. coli L-RhI, and the other part interacting with the 4, 5, and 6 positions is similar to D-XI. In E. coli L-RhI, the beta1-alpha1 loop creates an unique hydrophobic pocket at the the 4, 5, and 6 positions, leading to the strictly recognition of L-rhamnose as the most suitable substrate, while in P. stutzeri L-RhI, there is no corresponding hydrophobic pocket where Phe66 from a neighbouring molecule merely forms hydrophobic interactions with the substrate, leading to the loose substrate recognition at the 4, 5, and 6 positions.

About this Structure

2I56 is a Single protein structure of sequence from Pseudomonas stutzeri. Full crystallographic information is available from OCA.

Reference

The structures of L-rhamnose isomerase from Pseudomonas stutzeri in complexes with L-rhamnose and D-allose provide insights into broad substrate specificity., Yoshida H, Yamada M, Ohyama Y, Takada G, Izumori K, Kamitori S, J Mol Biol. 2007 Feb 2;365(5):1505-16. Epub 2006 Nov 6. PMID:17141803

Page seeded by OCA on Thu Mar 20 17:25:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools