1l9e

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1l9e.jpg|left|200px]]<br /><applet load="1l9e" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1l9e.jpg|left|200px]]
-
caption="1l9e, resolution 1.85&Aring;" />
+
 
-
'''Role of Histidine 269 in Catalysis by Monomeric Sarcosine Oxidase'''<br />
+
{{Structure
 +
|PDB= 1l9e |SIZE=350|CAPTION= <scene name='initialview01'>1l9e</scene>, resolution 1.85&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Sarcosine_oxidase Sarcosine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.1 1.5.3.1]
 +
|GENE=
 +
}}
 +
 
 +
'''Role of Histidine 269 in Catalysis by Monomeric Sarcosine Oxidase'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1L9E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=IMD:'>IMD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Sarcosine_oxidase Sarcosine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.1 1.5.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L9E OCA].
+
1L9E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L9E OCA].
==Reference==
==Reference==
-
Monomeric sarcosine oxidase: role of histidine 269 in catalysis., Zhao G, Song H, Chen ZW, Mathews FS, Jorns MS, Biochemistry. 2002 Aug 6;41(31):9751-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12146941 12146941]
+
Monomeric sarcosine oxidase: role of histidine 269 in catalysis., Zhao G, Song H, Chen ZW, Mathews FS, Jorns MS, Biochemistry. 2002 Aug 6;41(31):9751-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12146941 12146941]
[[Category: Bacillus sp.]]
[[Category: Bacillus sp.]]
[[Category: Sarcosine oxidase]]
[[Category: Sarcosine oxidase]]
Line 25: Line 34:
[[Category: oxidase]]
[[Category: oxidase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:42:50 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:28:14 2008''

Revision as of 10:28, 20 March 2008

Image:1l9e.jpg


PDB ID 1l9e

Drag the structure with the mouse to rotate
, resolution 1.85Å
Ligands: , and
Activity: Sarcosine oxidase, with EC number 1.5.3.1
Coordinates: save as pdb, mmCIF, xml



Role of Histidine 269 in Catalysis by Monomeric Sarcosine Oxidase


Overview

Conservative mutation of His269 (to Asn, Ala, or Gln) does not-significantly affect the expression of monomeric sarcosine oxidase (MSOX), covalent flavinylation, the physicochemical properties of bound FAD, or the overall protein structure. Turnover with sarcosine and the limiting rate of the reductive half-reaction with L-proline at pH 8.0 are, however, nearly 2 orders of magnitude slower than that with with wild-type MSOX. The crystal structure of the His269Asn complex with pyrrole-2-carboxylate shows that the pyrrole ring of the inhibitor is displaced as compared with wild-type MSOX. The His269 mutants all form charge-transfer complexes with pyrrole-2-carboxylate or methylthioacetate, but the charge-transfer bands are shifted to shorter wavelengths (higher energy) as compared with wild-type MSOX. Both wild-type MSOX and the His269Asn mutant bind the zwitterionic form of L-proline. The E(ox).L-proline complex formed with the His269Asn mutant or wild-type MSOX contains an ionizable group (pK(a) = 8.0) that is required for conversion of the zwitterionic L-proline to the reactive anionic form, indicating that His269 is not the active-site base. We propose that the change in ligand orientation observed upon mutation of His269 results in a less than optimal overlap of the highest occupied orbital of the ligand with the lowest unoccupied orbital of the flavin. The postulated effect on orbital overlap may account for the increased energy of charge-transfer bands and the slower rates of electron transfer observed for mutant enzyme complexes with charge-transfer ligands and substrates, respectively.

About this Structure

1L9E is a Single protein structure of sequence from Bacillus sp.. Full crystallographic information is available from OCA.

Reference

Monomeric sarcosine oxidase: role of histidine 269 in catalysis., Zhao G, Song H, Chen ZW, Mathews FS, Jorns MS, Biochemistry. 2002 Aug 6;41(31):9751-64. PMID:12146941

Page seeded by OCA on Thu Mar 20 12:28:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1l9e"
Personal tools