1wva

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
|PDB= 1wva |SIZE=350|CAPTION= <scene name='initialview01'>1wva</scene>, resolution 1.94&Aring;
|PDB= 1wva |SIZE=350|CAPTION= <scene name='initialview01'>1wva</scene>, resolution 1.94&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=S2C:S-2-(BORONOETHYL)-L-CYSTEINE'>S2C</scene>
+
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=S2C:S-2-(BORONOETHYL)-L-CYSTEINE'>S2C</scene>
-
|ACTIVITY= [http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1]
+
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </span>
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1wvb|1WVB]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wva OCA], [http://www.ebi.ac.uk/pdbsum/1wva PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wva RCSB]</span>
}}
}}
Line 30: Line 33:
[[Category: Rodriguez, P C.]]
[[Category: Rodriguez, P C.]]
[[Category: Sabio, G.]]
[[Category: Sabio, G.]]
-
[[Category: MN]]
 
-
[[Category: S2C]]
 
[[Category: bec inhibitor]]
[[Category: bec inhibitor]]
[[Category: hydrolase]]
[[Category: hydrolase]]
[[Category: twinned crystal]]
[[Category: twinned crystal]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:01:57 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:41:28 2008''

Revision as of 21:41, 30 March 2008


PDB ID 1wva

Drag the structure with the mouse to rotate
, resolution 1.94Å
Ligands: ,
Activity: Arginase, with EC number 3.5.3.1
Related: 1WVB


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of human arginase I from twinned crystal


Overview

Human arginase I is a potential target for therapeutic intervention in diseases linked to compromised l-arginine homeostasis. Here, we report high-affinity binding of the reaction coordinate analogue inhibitors 2(S)-amino-6-boronohexanoic acid (ABH, Kd = 5 nM) and S-(2-boronoethyl)-l-cysteine (BEC, Kd = 270 nM) to human arginase I, and we report x-ray crystal structures of the respective enzyme-inhibitor complexes at 1.29- and 1.94-A resolution determined from crystals twinned by hemihedry. The ultrahigh-resolution structure of the human arginase I-ABH complex yields an unprecedented view of the binuclear manganese cluster and illuminates the structural basis for nanomolar affinity: bidentate inner-sphere boronate-manganese coordination interactions and fully saturated hydrogen bond networks with inhibitor alpha-amino and alpha-carboxylate groups. These interactions are therefore implicated in the stabilization of the transition state for l-arginine hydrolysis. Electron density maps also reveal that active-site residue H141 is protonated as the imidazolium cation. The location of H141 is such that it could function as a general acid to protonate the leaving amino group of l-ornithine during catalysis, and this is a revised mechanistic proposal for arginase. This work serves as a foundation for studying the structural and chemical biology of arginase I in the immune response, and we demonstrate the inhibition of arginase activity by ABH in human and murine myeloid cells.

About this Structure

1WVA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response., Di Costanzo L, Sabio G, Mora A, Rodriguez PC, Ochoa AC, Centeno F, Christianson DW, Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13058-63. Epub 2005 Sep 2. PMID:16141327

Page seeded by OCA on Mon Mar 31 00:41:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools